Post-translational modifications (PTMs)—the chemical changes that proteins undergo following biosynthesis—account for most protein forms, or proteoforms. Indeed, according to conservative estimates, there are 1 million proteoforms, 90% of which are believed to be PTM-derived proteoforms. Estimates for the number of proteoforms and the percentage of PTM-derived proteoforms sometimes range quite a bit higher, depending on how the proteoforms are defined.1
The many PTM-derived proteoforms are important because they add greatly to the functional diversity of the proteome. They correspond to dynamic, labile, and often cell- or tissue-specific PTMs that regulate cellular pathways. Presumably, these PTMs have much to tell researchers in the life sciences. But these researchers will have to listen closely. Many PTMs are rare, subtle, and fleeting.
A more fundamental issue is that there are many types of PTMs. Indeed, there are over 400. About 90% of PTMs, however, are of just three types—phosphorylation, acetylation, and ubiquitination. Other major PTM types include glycosylation, succinylation, methylation, malonylation, SUMOylation, palmitoylation, myristoylation, prenylation, and sulfation.2 PTMs can be simple or complex. Examples of the latter include glycosylation and polyubiquitination. These PTMs may result in linear-chain and branched-chain structures.
Although the proteome is vast, it needn’t overwhelm. And although it is full of intricacy, it needn’t bewilder. The proteome may be studied with an expanding array of tools and technologies. Many of these tools and technologies are described in this article.
Accelerating proteoform discovery
Aaron M. Robitaille, PhD, director of marketing, mass spectrometry, Thermo Fisher Scientific, notes that the first PTM was discovered over 100 years ago.3 He adds that it is only now that we are starting to appreciate how many proteoforms exist.
Typically, PTMs are analyzed in both temporal and spatial terms to clarify how they regulate cellular function. According to Robitaille, a classic example is phosphorylation, where the addition or subtraction of phosphate to an amino acid can activate or deactivate a protein. This PTM can serve as a kind of on/off switch.
The sample enrichment requirement prior to analysis to increase detection of low-abundance proteins and/or to reduce sample complexity is a key challenge. “Proteoforms can be transient and rare,” Robitaille notes. “They also can become dysregulated in disease and thus are important therapeutic targets. But small clinical samples such as biopsies present a limitation for enrichment.”
According to Robitaille, mass spectrometry (MS) offers the best sensitivity and specificity to study PTMs. He notes that once a standardized MS assay is developed, it can be deployed globally in multiple settings and produce the same quantitative results.
Robitaille indicates that the generation of Selective Temporal Overview of Resonant Ions (STORI) plots4 can be facilitated by an MS solution called Thermo Scientific Direct Mass Technology mode. Moreover, it can enable precise measurements of heavily modified proteoforms, such as those produced from glycosylation processes that are too complex to resolve using customary methods.
Traditionally, affinity reagents such as antibodies or aptamers must be generated for each specific PTM modification site and verified for specificity, requiring enormous amounts of reagents. In contrast, high-resolution accurate-mass (HRAM) instrumentation enables the characterization of proteoforms in their naïve state as well as the discovery of new PTMs with specific site localization. This fit-for-purpose MS technology is designed specifically to help scale to the level of 6 million proteoforms.
“We are analyzing single proteoforms without the need for enrichment,” Robitaille emphasizes. “The incredible sensitivity shows the heterogeneity of the biological system.” In the future, a range of MS-based assays including enzymatic activity, thermal shift, and protein degradation (PROTAC) studies will potentially address the functional effect of PTMs on protein-based activity.
“MS instruments do not directly measure function,” Robitaille points out. “You need a properly controlled experimental design that can take advantage of the sensitive and specific MS readout to understand function. Many PTMs are understudied due to a lack of enrichment tools or affinity reagents, representing a key area where MS empowered by Thermo Scientific Orbitrap technology and Direct Mass Technology mode can play a major role.”
Grappling with glycobiology
The rise of therapeutic antibodies results in the need to characterize lot-to-lot glycan profiles. “It is well known how glycans influence antibodies’ therapeutic potency,” says Anthony Person, PhD, senior director, Protein Business Unit, Bio-Techne. For example, certain immunoglobulin G1 antibodies rely on the Fc-mediated immune effector function, known as antibody-dependent cellular cytotoxicity (ADCC), as a central way to deplete tumor cells. Core fucosylation on N-glycans on antibody heavy chains directly influences the binding affinity of the antibody’s Fc portion to the FcgRIIIa receptor present on immune effector cells like natural killer cells. Generally, antibodies without this core fucosylation can bind to FcgRIIIa with higher affinity, resulting in higher ADCC and efficacy.
The cell culture step is central to having the desired glycan profiles on recombinant proteins. Commonly, immature N-glycans, like high-mannose N-glycans, lack terminal sialyation and galactosylation and are more easily cleared in vivo, resulting in lower antibody efficacy. High-mannose N-glycans result from suboptimal CHO or HEK293 cell culture parameters.
“Although MS analysis is still the gold standard for characterization, glycan profiling can be infeasible,” Person warns. “We produce over 6,000 research-grade, non-antibody protein products and do not have the ability to run them all through MS due to the low throughput and high cost.”
Recently developed benchtop techniques rely on Bio-Techne’s catalog of glycobiology enzymes and substrates to footprint both N– and O-linked glycans. “We can use neuraminidase to remove sialic acid or FUCA1 to remove fucose followed by fucosyltransferases and sialyltransferases to add fluorescently labeled sugars to glycans,” Person relates. “Labeled recombinant proteins can then be run on SDS-PAGE gels, and differences in sialylation, galactosylation, or fucosylation can be easily visualized to compare glycan footprints.”
The approach was used to investigate differences in glycosylation patterns of SARS-CoV-2 spike proteins made in insect, CHO, and HEK293 production hosts.
The original SARS-CoV-2 canonical spike protein comprising the receptor binding domain (RBD) that was produced in insect hosts (Sf21 or Tn5) possessed generally high-mannose, immature N-glycans with more immature core-1 O-glycans. CHO host-produced RBD proteins showed N-glycans that were terminally galactosylated without terminal sialylation with core-1 O-glycans. The most mature RBD glycan profiles were seen on the HEK293 host-produced proteins that were both terminal sialylated on N-glycans and also displayed core-2 O-glycans.
“The finding that the original SARS-CoV-2 spike protein contains 22 N-glycosylation sites emphasizes glycobiology’s complexity,” Person declares.
“The importance of PTMs, particularly glycosylation, has been established in biopharmaceutical manufacturing,” says Nan Lin, PhD, director, New Technologies and Service Applications, Cytiva. Variants of glycosylation, together with variants in charge and size, are among the key aspects of recombinant protein microheterogeneity.
Controlling microheterogeneity to advance PTM control has become essential in implementing quality by design (QbD) and in meeting biosimilarity criteria. In recent years, industrial and academic researchers have made significant progress in controlling and modulating glycosylation via media and process optimization. “Glycosylation modulation,” Lin remarks, “has gained more focus not only in fed-batch but also in perfusion processes in recent years.”
Current methods are mainly based on rather lengthy workflows—collecting samples, purification, and analysis. High-throughput, low-sample-volume, and low-protein-quantity PTM analytical methods remain the challenge.
“High-throughput analytical methods, coupled with high-throughput cell culture platforms such as microbioreactors would enable assessment of PTMs in very early steps in cell line and process development,” Lin suggests. “Online/at-line analyses in an integrated, fully automated system has become increasingly discussed and developed for online PTM data monitoring.”
Numerous chip- and kit-based rapid glycosylation analysis methods are available and make good tools for bioprocess development, especially where analytical capabilities are not readily available.
“Several research groups have proposed to characterize global cellular PTM characterization, including glycosylation, phosphorylation, and ubiquitination, as part of understanding and controlling cell physiology,” Lin notes. “Such groundbreaking work would provide effective cell engineering targets and process monitoring endpoints in the future.”
Emerging biopharmaceutical molecules, including Fc-fusion and bispecific proteins, have gained presence in many pharmaceutical companies’ development pipelines. Many new molecules have unique structures and PTMs required by mechanisms of action.
“To be able to control PTMs of the new molecules early in development will be critical for future QbD processes,” Lin stresses. “Novel host cell lines for producing therapeutic proteins are on the horizon. Human origin or glycoengineered CHO host cell lines may be able to produce more human-like glycosylation patterns, and to achieve better glycosylation control.”
Exploring new ways to study low-abundance PTMs
“In vertebrates, the investigative focus has primarily been on serine, threonine, and tyrosine phosphorylation, but mounting evidence suggests that phosphorylation of other, ‘noncanonical’ amino acids also regulates critical aspects of cell biology,” reports a scientific team led by Claire E. Eyers, PhD, professor of biological mass spectrometry at the University of Liverpool.
“Eyers’ use of strong anion exchange-mediated phosphoproteomics to detect noncanonical phosphorylation indicated that the number of unique noncanonical phosphosites is approximately one-third of the number of observed canonical phosphosites,” comments Cristina Martin-Granados, PhD, research area scientific lead, Cell Signaling, Abcam.5 Although the numbers presented by Eyers and colleagues need to be firmed up, they are already encouraging researchers to consider broadening their views of the phosphorylation landscape.
According to Martin-Granados, low-abundance PTMs can make detection by antibody-based approaches difficult. Enrichment of a specific PTM by immunoprecipitation or by ion exchange, immobilized metal ion affinity, or immunoaffinity chromatography can help overcome low-stoichiometry challenges.
She emphasizes that dynamic and frequently transient PTMs require stringent positive and negative experimental controls if results are to be correctly interpreted. Since many PTMs are the aftermath of enzymatic reactions, uncontrolled enzymatic activity in sample processing can affect them.
“Antibodies are essential tools for detection and enrichment,” Martin-Granados remarks. “The challenge in developing highly specific antibodies with exquisite binding affinity is the small size of the PTM chemical moieties, similarities in some chemical structures, and poor antigenicity. Polyclonal antibodies present serious drawbacks in delivering reproducible and reliable data. To avoid these drawbacks, it may be necessary to switch to highly functional, reliable, and renewable recombinant monoclonals.”
Computational methods for predicting PTMs are attracting considerable attention. For example, AlphaFold, an artificial intelligence platform, made the news when it demonstrated its prowess in predicting unsolved protein structures from amino acid sequences. However, as Martin-Granados explains, AlphaFold2 does not yet consider the impact of PTMs on protein structure. Fortunately, databases on protein PTMs and predictive computational tools are available.
Proximity ligation assay (PLA), an antibody-dependent, fast, and highly sensitive immunoassay technology, can be used to detect PTMs, allowing for identification of several PTMs in a specific target.6,7 PLA technology can be used in combination with immunocytochemistry/immunofluorescence analysis and fluorescence immunohistochemistry analysis to study protein localizations and validate potential biomarkers for clinical diagnostic testing.
Genetic code expansion enables site-specific placement of functionally masked unnatural amino acids into proteins. These unnatural amino acids may remain inert until they are activated by a signal of some kind, that is, by a particular kind of illumination or by a small molecule. This provides rapid and temporal external control over addition and removal of PTMs, eliminating compensatory mechanisms that arise by slow conventional approaches, and it is expected to significantly increase the understanding of transient, dynamic PTM events.8
“Sensitivity and the dynamic range for detection of low-abundance PTMs need improvement as well as accurate, quantitative methods for studying dynamics and for analysis of less-well-known or newly identified PTMs,” Martin-Granados adds. “The relevance of multisite, cooperative PTMs highlights the need to develop strategies for full-spectrum identification of PTMs.”
Meeting characterization challenges
Previously, PTMs were thought of in binary terms—as either activating or inactivating, based on the particular modification and pathway. “Now, we understand to a greater degree how subtle changes in PTMs can modulate activity and signals,” says Carl Ascoli, PhD, chief science officer, Rockland Immunochemicals.
Although PTMs of proteins increase the functional diversity of the proteome to adapt to rapid changes in the environment, this diversity places strain on the availability of detection and characterization antibodies to certain modifications.
“Consider two characterization challenges: those involving ubiquitination, and those involving epigenetics,” Ascoli suggests. “Ubiquitination is a complex, multistep, reversible process that is highly regulated by the sequential action of very specific enzymes that add or remove ubiquitin. These enzymes may add monoubiquitin, polyubiquitin, and branched-chain ubiquitin at one or more targets sites on a given protein. This complexity makes understanding the machinery of ubiquitin in the laboratory a difficult process.”
“Epigenetic modifications, such as PTMs on histones, can be numerous, diverse, subtle, and transient, and they can work in combination,” Ascoli continues. Different cellular processes are affected depending on whether a particular amino acid is modified by a single, double, or triple methylation event, or whether it is unmethylated. Subtle variations in PTMs can result from changes due to environment, diet, disease, stress, or drug therapy.
Immunoassays using specific antibodies to PTMs generated in context with the surrounding amino acids on an enzyme are valuable tools for detection and characterization whether experiments are conducted in vitro or with biological systems involving immunofluorescence microscopy of organoids or whole animal in vivo imaging.
According to Ascoli, antibodies to AKT pS473, MEK pT386, or STAT3 pY705 have been invaluable in elucidating regulatory pathways and exploring the efficacy of drugs in both benchtop and biological experiments. He adds, however, that PTMs are more diverse and abundant than well-characterized antibodies.
Understanding the function of PTMs requires a more universal detection strategy. For instance, it may be necessary to rely on physicochemical detection methods such as MS analysis. Methods that look at entire proteins may be especially useful. Variations that increase accuracy and add context to the MS data include MALDI-MS, ESI-MS, and tandem MS.
“Detection or analysis methods that are based on protein binding directly or indirectly to DNA or RNA are of interest and will continue to evolve,” Ascoli predicts. “While assays like CUT&RUN, CUT&TAG, and more recent variations called TIP-seq and MULTI-CUT&TAG are themselves dependent on antibodies that bind to the protein that binds nucleic acids, the information that these assays provide is much richer in context.”
1. Aebersold R, Agar JN, Amster IJ, et al. How many human proteoforms are there? Nat. Chem. Biol. 2018; 14: 206–214. DOI: 10.1038/nchembio.2576.
2. Ramazi S, Zahiri J. Post-translational modifications in proteins: resources, tools and prediction methods. Database (Oxford) 2021; 2021: baab012. DOI: 10.1093/database/baab012.
3. Levene P, Alsberg C. The cleavage products of vitellin. J. Biol. Chem. 1906; 2: 127–133.
4. Kafader JO, Beu SC, Early BP, et al. STORI Plots Enable Accurate Tracking of Individual Ion Signals. J. Am. Soc. Mass Spectrom. 2019; 30: 2200–2203. DOI: 10.1007/s13361-019-02309-0.
5. Hardman G, Perkins S, Brownridge PJ, et al. Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation. EMBO J. 2019; 38: e100847. DOI: 10.15252/embj.2018100847.
6. Tong QH, Tao T, Xie LQ, Lu HJ. ELISA–PLA: A novel hybrid platform for the rapid, highly sensitive and specific quantification of proteins and post-translational modifications. Biosens. Bioelectron. 2016; 80: 385–391. DOI: 10.1016/j.bios.2016.02.006.
7. de Oliviera FMS, Mereiter S, Lönn P, et al. Detection of post-translational modifications using solid-phase proximity ligation assay. N. Biotechnol. 2018; 45: 51–59. DOI: 10.1016/j.nbt.2017.10.005.
8. Zhou W, Deiters A. Chemogenetic and optogenetic control of post-translational modifications through genetic code expansion. Curr. Opin. Chem. Biol. 2021; 63: 123–131. DOI: 10.1016/j.cbpa.2021.02.016.
An economist digging below the surface of an IMF report has found something that should shock the Western bloc out of any false confidence in its unsurpassed global economic clout...
G7 leaders meeting on June 28, 2022, at Schloss Elmau in Krün, Germany. (White House/Adam Schultz)
Last summer, the Group of 7 (G7), a self-anointed forum of nations that view themselves as the most influential economies in the world, gathered at Schloss Elmau, near Garmisch-Partenkirchen, Germany, to hold their annual meeting. Their focus was punishing Russia through additional sanctions, further arming of Ukraine and the containment of China.
At the same time, China hosted, through video conference, a gathering of the BRICS economic forum. Comprised of Brazil, Russia, India, China and South Africa, this collection of nations relegated to the status of so-called developing economies focused on strengthening economic bonds, international economic development and how to address what they collectively deemed the counter-productive policies of the G7.
In early 2020, Russian Deputy Foreign Minister Sergei Ryabkov had predicted that, based upon purchasing power parity, or PPP, calculations projected by the International Monetary Fund, BRICS would overtake the G7 sometime later that year in terms of percentage of the global total.
(A nation’s gross domestic product at purchasing power parity, or PPP, exchange rates is the sum value of all goods and services produced in the country valued at prices prevailing in the United States and is a more accurate reflection of comparative economic strength than simple GDP calculations.)
Then the pandemic hit and the global economic reset that followed made the IMF projections moot. The world became singularly focused on recovering from the pandemic and, later, managing the fallout from the West’s massive sanctioning of Russia following that nation’s invasion of Ukraine in February 2022.
The G7 failed to heed the economic challenge from BRICS, and instead focused on solidifying its defense of the “rules based international order” that had become the mantra of the administration of U.S. President Joe Biden.
Since the Russian invasion of Ukraine, an ideological divide that has gripped the world, with one side (led by the G7) condemning the invasion and seeking to punish Russia economically, and the other (led by BRICS) taking a more nuanced stance by neither supporting the Russian action nor joining in on the sanctions. This has created a intellectual vacuum when it comes to assessing the true state of play in global economic affairs.
U.S. President Joe Biden in virtual call with G7 leaders and Ukrainian President Volodymyr Zelenskyy, Feb. 24. (White House/Adam Schultz)
It is now widely accepted that the U.S. and its G7 partners miscalculated both the impact sanctions would have on the Russian economy, as well as the blowback that would hit the West.
“when this started a year ago, all the talk was the sanctions are going to cripple Russia. They’re going to be just out of business and riots in the street absolutely hasn’t worked …[w]ere they the wrong sanctions? Were they not applied well? Did we underestimate the Russian capacity to circumvent them? Why have the sanctions regime not played a bigger part in this conflict?”
It should be noted that the IMF calculated that the Russian economy, as a result of these sanctions, would contract by at least 8 percent. The real number was 2 percent and the Russian economy — despite sanctions — is expected to grow in 2023 and beyond.
This kind of miscalculation has permeated Western thinking about the global economy and the respective roles played by the G7 and BRICS. In October 2022, the IMF published its annual World Economic Outlook (WEO), with a focus on traditional GDP calculations. Mainstream economic analysts, accordingly, were comforted that — despite the political challenge put forward by BRICS in the summer of 2022 — the IMF was calculating that the G7 still held strong as the leading global economic bloc.
In January 2023 the IMF published an update to the October 2022 WEO, reinforcing the strong position of the G7. According to Pierre-Olivier Gourinchas, the IMF’s chief economist, the “balance of risks to the outlook remains tilted to the downside but is less skewed toward adverse outcomes than in the October WEO.”
This positive hint prevented mainstream Western economic analysts from digging deeper into the data contained in the update. I can personally attest to the reluctance of conservative editors trying to draw current relevance from “old data.”
Fortunately, there are other economic analysts, such as Richard Dias of Acorn Macro Consulting, a self-described “boutique macroeconomic research firm employing a top-down approach to the analysis of the global economy and financial markets.”
Rather than accept the IMF’s rosy outlook as gospel, Dias did what analysts are supposed to do — dig through the data and extract relevant conclusions.
After rooting through the IMF’s World Economic Outlook Data Base, Dias conducted a comparative analysis of the percentage of global GDP adjusted for PPP between the G7 and BRICS, and made a surprising discovery: BRICS had surpassed the G7.
This was not a projection, but rather a statement of accomplished fact:
BRICS was responsible for 31.5 percent of the PPP-adjusted global GDP, while the G7 provided 30.7 percent.
Making matters worse for the G7, the trends projected showed that the gap between the two economic blocs would only widen going forward.
The reasons for this accelerated accumulation of global economic clout on the part of BRICS can be linked to three primary factors:
residual fallout from the Covid-19 pandemic,
blowback from the sanctioning of Russia by the G7 nations in the aftermath of the Russian invasion of Ukraine and a growing resentment among the developing economies of the world to G7 economic policies and
priorities which are perceived as being rooted more in post-colonial arrogance than a genuine desire to assist in helping nations grow their own economic potential.
It is true that BRICS and G7 economic clout is heavily influenced by the economies of China and the U.S., respectively. But one cannot discount the relative economic trajectories of the other member states of these economic forums. While the economic outlook for most of the BRICS countries points to strong growth in the coming years, the G7 nations, in a large part because of the self-inflicted wound that is the current sanctioning of Russia, are seeing slow growth or, in the case of the U.K., negative growth, with little prospect of reversing this trend.
Moreover, while G7 membership remains static, BRICS is growing, with Argentina and Iran having submitted applications, and other major regional economic powers, such as Saudi Arabia, Turkey and Egypt, expressing an interest in joining. Making this potential expansion even more explosive is the recent Chinese diplomatic achievement in normalizing relations between Iran and Saudia Arabia.
Diminishing prospects for the continued global domination by the U.S. dollar, combined with the economic potential of the trans-Eurasian economic union being promoted by Russia and China, put the G7 and BRICS on opposing trajectories. BRICS should overtake the G7 in terms of actual GDP, and not just PPP, in the coming years.
But don’t hold your breath waiting for mainstream economic analysts to reach this conclusion. Thankfully, there are outliers such as Richard Dias and Acorn Macro Consulting who seek to find new meaning from old data.
The U.S. Centers for Disease Control and Prevention (CDC) made at least 25 statistical or numerical errors during the COVID-19 pandemic, and the overwhelming majority exaggerated the severity of the pandemic, according to a new study.
Researchers who have been tracking CDC errors compiled 25 instances where the agency offered demonstrably false information. For each instance, they analyzed whether the error exaggerated or downplayed the severity of COVID-19.
“The CDC has expressed significant concern about COVID-19 misinformation. In order for the CDC to be a credible source of information, they must improve the accuracy of the data they provide,” the authors wrote.
The CDC did not respond to a request for comment.
Most Errors Involved Children
Most of the errors were about COVID-19’s impact on children.
In mid-2021, for instance, the CDC claimed that 4 percent of the deaths attributed to COVID-19 were kids. The actual percentage was 0.04 percent. The CDC eventually corrected the misinformation, months after being alerted to the issue.
CDC Director Dr. Rochelle Walensky falsely told a White House press briefing in October 2021 that there had been 745 COVID-19 deaths in children, but the actual number, based on CDC death certificate analysis, was 558.
Walensky and other CDC officials also falsely said in 2022 that COVID-19 was a top five cause of death for children, citing a study that gathered CDC data instead of looking at the data directly. The officials have not corrected the false claims.
Other errors include the CDC claiming in 2022 that pediatric COVID-19 hospitalizations were “increasing again” when they’d actually peaked two weeks earlier; CDC officials in 2023 including deaths among infants younger than 6 months old when reporting COVID-19 deaths among children; and Walensky on Feb. 9, 2023, exaggerating the pediatric death toll before Congress.
“These errors suggest the CDC consistently exaggerates the impact of COVID-19 on children,” the authors of the study said.
WINSTON-SALEM, N.C. – March 24, 2023 – Researchers at Wake Forest University School of Medicine have been awarded a five-year, $7.5 million grant from the National Institutes of Health (NIH) Helping End Addiction Long-term (HEAL) initiative.
Credit: Wake Forest University School of Medicine
WINSTON-SALEM, N.C. – March 24, 2023 – Researchers at Wake Forest University School of Medicine have been awarded a five-year, $7.5 million grant from the National Institutes of Health (NIH) Helping End Addiction Long-term (HEAL) initiative.
The NIH HEAL initiative, which launched in 2018, was created to find scientific solutions to stem the national opioid and pain public health crises. The funding is part of the HEAL Data 2 Action (HD2A) program, designed to use real-time data to guide actions and change processes toward reducing overdoses and improving opioid use disorder treatment and pain management.
With the support of the grant, researchers will create a data infrastructure support center to assist HD2A innovation projects at other institutions across the country. These innovation projects are designed to address gaps in four areas—prevention, harm reduction, treatment of opioid use disorder and recovery support.
“Our center’s goal is to remove barriers so that solutions can be more streamlined and rapidly distributed,” said Meredith C.B. Adams, M.D., associate professor of anesthesiology, biomedical informatics, physiology and pharmacology, and public health sciences at Wake Forest University School of Medicine.
By monitoring opioid overdoses in real time, researchers will be able to identify trends and gaps in resources in local communities where services are most needed.
“We will collect and analyze data that will inform prevention and treatment services,” Adams said. “We’re shifting chronic pain and opioid care in communities to quickly offer solutions.”
The center will also develop data related resources, education and training related to substance use, pain management and the reduction of opioid overdoses.
According to the CDC, there was a 29% increase in drug overdose deaths in the U.S. in 2020, and nearly 75% of those deaths involved an opioid.
“Given the scope of the opioid crises, which was only exacerbated by the COVID-19 pandemic, it’s imperative that we improve and create new prevention strategies,” Adams said. “The funding will create the infrastructure for rapid intervention.”