4.7 Article

Divergent Antibody Repertoires Found for Omicron versus Wuhan SARS-CoV-2 Strains Using Ig-MS

期刊

JOURNAL OF PROTEOME RESEARCH
卷 21, 期 12, 页码 2987-2997

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.2c00514

关键词

antibodies; SARS-CoV-2; Omicron variant; COVID-19; Ig-MS; serology

资金

  1. NIAID, NIH [HHSN272201400008C]
  2. National Institute of Health, National Institute of General Medical Sciences [P41 GM108569]
  3. Research Corporation [27372]
  4. Walder Foundation's Chicago Coronavirus Assessment Network (Chicago CAN) Initiative Grant [SCI16, 21-00147, 21-00650]

向作者/读者索取更多资源

SARS-CoV-2 Omicron and its subvariants are highly transmissible and resistant to neutralization by antibodies from vaccination and previous infections. The study used the Ig-MS platform to investigate the antibody response to booster shots and natural infection, as well as the ability of antibodies generated against Omicron variant to bind to different RBDs. The results showed that booster shots increase antibody titers and elicit an Omicron-specific response, while vaccination and infection together generate variant-specific antibodies.
SARS-CoV-2 Omicron (B.1.1.529) and its subvariants are currently the most common variants of concern worldwide, featuring numerous mutations in the spike protein and elsewhere that collectively make Omicron variants more transmissible and more resistant to antibody-mediated neutralization provided by vaccination, previous infections, and monoclonal antibody therapies than their predecessors. We recently reported the creation and characterization of Ig-MS, a new mass spectrometry-based serology platform that can define the repertoire of antibodies against an antigen of interest at single proteoform resolution. Here, we applied Ig-MS to investigate the evolution of plasma antibody repertoires against the receptor-binding domain (RBD) of SARS-CoV-2 in response to the booster shot and natural viral infection. We also assessed the capacity for antibody repertoires generated in response to vaccination and/or infection with the Omicron variant to bind to both Wuhan-and Omicron-RBDs. Our results show that (1) the booster increases antibody titers against both Wuhan-and Omicron-RBDs and elicits an Omicron-specific response and (2) vaccination and infection act synergistically in generating anti-RBD antibody repertoires able to bind both Wuhan-and Omicron-RBDs with variant-specific antibodies.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

Article Biochemical Research Methods

Next-Generation Serology by Mass Spectrometry: Readout of the SARS-CoV-2 Antibody Repertoire

Rafael D. Melani, Benjamin J. Des Soye, Jared O. Kafader, Eleonora Forte, Michael Hollas, Voislav Blagojevic, Fernanda Negrao, John P. McGee, Bryon Drown, Cameron Lloyd-Jones, Henrique S. Seckler, Jeannie M. Camarillo, Philip D. Compton, Richard D. LeDuc, Bryan Early, Ryan T. Fellers, Byoung-Kyu Cho, Basil Baby Mattamana, Young Ah Goo, Paul M. Thomas, Michelle K. Ash, Pavan P. Bhimalli, Lena Al-Harthi, Beverly E. Sha, Jeffrey R. Schneider, Neil L. Kelleher

Summary: Ig-MS is a novel serological readout capturing the immunoglobulin repertoire at molecular resolution without sequencing of B cells. This method can be used to assess exposure or immunity to a pathogen.

JOURNAL OF PROTEOME RESEARCH (2022)

Article Biochemistry & Molecular Biology

The Human Proteoform Atlas: a FAIR community resource for experimentally derived proteoforms

Michael A. R. Hollas, Matthew T. Robey, Ryan T. Fellers, Richard D. LeDuc, Paul M. Thomas, Neil L. Kelleher

Summary: The Human Proteoform Atlas is an online repository storing experimentally verified human proteoforms, using a FAIR system to assign persistent identifiers and facilitate tracking and organization. Users can submit new proteoforms via email, and future iterations will help in studying and organizing these protein molecules further.

NUCLEIC ACIDS RESEARCH (2022)

Article Microbiology

β-catenin regulates HIV latency and modulates HIV reactivation

Hannah J. Barbian, Melanie S. Seaton, Srinivas D. Narasipura, Jennillee Wallace, Reshma Rajan, Beverly E. Sha, Lena Al-Harthi

Summary: Latency is the main obstacle towards an HIV cure, and targeting multiple latency maintenance pathways is essential. In this study, beta-catenin, a transcriptional co-activator and central mediator of Wnt signaling, is identified as a regulator of HIV latency. Inhibiting or activating the beta-catenin pathway can reactivate or repress HIV, and it also enhances or inhibits the activity of other HIV latency reversing agents.

PLOS PATHOGENS (2022)

Article Biochemistry & Molecular Biology

Revving an Engine of Human Metabolism: Activity Enhancement of Triosephosphate Isomerase via Hemi-Phosphorylation

Luis F. Schachner, Benjamin Des Soye, Soo Ro, Grace E. Kenney, Ashley N. Ives, Taojunfeng Su, Young Ah Goo, Michael C. Jewett, Amy C. Rosenzweig, Neil L. Kelleher

Summary: The phosphorylation of triosephosphate isomerase (TPI) enhances its activity and facilitates substrate binding to the active site. Hetero-dimerization and subunit asymmetry are key features of TPI, and tetramerization plays a crucial role in enzymatic regulation. This study highlights the importance of studying endogenous proteoforms for understanding the functional role of post-translational modifications (PTMs).

ACS CHEMICAL BIOLOGY (2022)

Article Multidisciplinary Sciences

Highly multiplexed, label-free proteoform imaging of tissues by individual ion mass spectrometry

Pei Su, John P. McGee, Kenneth R. Durbin, Michael A. R. Hollas, Manxi Yang, Elizabeth K. Neumann, Jamie L. Allen, Bryon S. Drown, Fatma Ayaloglu Butun, Joseph B. Greer, Bryan P. Early, Ryan T. Fellers, Jeffrey M. Spraggins, Julia Laskin, Jeannie M. Camarillo, Jared O. Kafader, Neil L. Kelleher

Summary: Imaging of proteoforms in human tissues is limited by low molecular specificity and proteome coverage. Proteoform imaging mass spectrometry (PiMS) overcomes these limitations by increasing the size limit for proteoform detection and identification, and revealing the spatial localization of proteoforms in tissues at high resolution.

SCIENCE ADVANCES (2022)

Article Chemistry, Analytical

Automated Control of Injection Times for Unattended Acquisition of Multiplexed Individual Ion Mass Spectra

John P. McGee, Michael W. Senko, Kevin Jooss, Benjamin J. Des Soye, Philip D. Compton, Neil L. Kelleher, Jared O. Kafader

Summary: Charge detection mass spectrometry (CDMS) is a method for detecting mass spectra of large and highly heterogeneous analytes. CDMS has been multiplexed on Orbitrap instruments to achieve Individual Ion Mass Spectrometry (I2MS). In this study, an automated method called Automatic Ion Control (AIC) was developed to adjust ion injection times in I2MS for image current detectors like the Orbitrap. AIC utilizes signal density in the m/z domain to adjust ions in real-time for sample adaptability, online separations, and ease of use. The technique was successfully applied to denatured and native proteins, producing high quality data without human intervention directly in the mass domain.

ANALYTICAL CHEMISTRY (2022)

Article Microbiology

Utility of the Signal-to-Cutoff Ratio and Antigen Index from Fourth- and Fifth-Generation HIV-1/HIV-2 Antigen/Antibody Assays for the Diagnosis of Acute HIV Infection: Applicability for Real-Time Use for Immediate Initiation of Antiretroviral Therapy

Elena Whitney, David Pitrak, Kathleen G. Beavis, Nicholas M. Moore, Shivanjali Shankaran, Ana Precy Abeleda, Jessica Schmitt, Beverly E. Sha

Summary: This study identifies the accuracy of using S/CO ratio and antigen index (Al) to improve the diagnosis accuracy of acute HIV infection (AHI). The results show that a threshold value of 3.78 for S/CO ratio and 2.83 for Al can provide high sensitivity and specificity in identifying AHI patients. However, there may still be false-positive results, indicating the possibility of biological false-positives.

JOURNAL OF CLINICAL MICROBIOLOGY (2022)

Article Chemistry, Physical

Electronic Structure of Heteronuclear Cerium-Platinum Clusters

Jarrett L. Mason, Caleb D. Huizenga, Manisha Ray, Jared O. Kafader, Caroline Chick Jarrold

Summary: The electronic structure of mixed Ce-Pt clusters has been studied experimentally and theoretically. The clusters exhibit unique magnetic and electron coupling properties, which have potential implications for the study of Ce-rich intermetallic materials.

JOURNAL OF PHYSICAL CHEMISTRY A (2023)

Article Biochemical Research Methods

Immunocomplexed Antigen Capture and Identification by Native Top-Down Mass Spectrometry

John P. McGee, Rafael D. Melani, Ben Des Soye, Derek Croote, Valerie Winton, Stephen R. Quake, Jared O. Kafader, Neil L. Kelleher

Summary: This study used native tandem mass spectrometry to probe antibody-antigen complexes and successfully characterized the molecular composition of protein antigens. The results demonstrated the potential of native top-down mass spectrometry as a platform for precise and thorough characterization of immunocomplexes, enabling the discovery of antigen proteoforms and their binding sites.

JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY (2023)

Article Mathematical & Computational Biology

Identification of Splice Variants and Isoforms in Transcriptomics and Proteomics

Taojunfeng Su, Michael A. R. Hollas, Ryan T. Fellers, Neil L. Kelleher

Summary: Alternative splicing plays a crucial role in regulating gene expression and protein diversity in eukaryotic cells. Traditional short-read RNA sequencing has been widely used for studying alternative splicing, but the emergence of long-read RNA sequencing and top-down mass spectrometry offers new opportunities to identify alternative splicing events and protein isoforms with higher accuracy. This review summarizes the recent improvements in short-read RNA sequencing and computational methods for alternative splicing analysis, as well as the approaches used in top-down proteomics to identify protein isoforms. However, future efforts are needed to further enhance the effectiveness, integration, and proteome coverage of alternative splicing events.

ANNUAL REVIEW OF BIOMEDICAL DATA SCIENCE (2023)

Article Biochemical Research Methods

Determining Collisional Cross Sections from Ion Decay with Individual Ion Mass Spectrometry

Nickolas P. Fisher, John P. McGee, Kyle P. Bowen, Michael Goodwin, Michael W. Senko, Neil L. Kelleher, Jared O. Kafader

Summary: Ion mobility spectrometry (IMS) measurements of collision cross section (CCS) provide valuable information about the structure of proteins in gas phase, which complements mass analysis. Methods for determining CCS without a dedicated IMS system have been developed for Fourier transform mass spectrometry (FT-MS) platforms. Individual ion mass spectrometry (IMS-M-2) allows charge detection and measures ion lifetimes throughout the detection event of FT-MS, enabling simultaneous determination of charge, mass, and CCS for proteins and complexes ranging in size from approximately 8 to approximately 232 kDa.

JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY (2023)

Meeting Abstract Biochemical Research Methods

Highly multiplexed label-free imaging of tissue proteoforms using individual ion mass spectrometry

Pei Su, John P. McGee, Kenneth R. Durbin, Michael A. Hollas, Ryan T. Fellers, Jeannie M. Camarillo, Jared O. Kafader, Neil L. Kelleher

MOLECULAR & CELLULAR PROTEOMICS (2022)

暂无数据