Evidence map›Paper›PMID 39434663›Full record

ArticleAnalytical chemistry2024

Direct Mapping of Polyclonal Epitopes in Serum by HDX-MS.

Clint Vorauer, Camila Boniche-Alfaro, Taylor Murphree, Tsutomu Matsui, Thomas Weiss, Bettina C Fries, Miklos Guttman

Abstract read
In one paragraph

Article in Analytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Clint VorauerDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington 98195, United States.
Camila Boniche-AlfaroDepartment of Medicine, Infectious Disease Division, Stony Brook University, Stony Brook, New York 11794, United States.
Taylor MurphreeDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington 98195, United States.
Tsutomu MatsuiStanford Synchrotron Radiation Laboratory, SLAC, Menlo Park, California 94025, United States.
Thomas WeissStanford Synchrotron Radiation Laboratory, SLAC, Menlo Park, California 94025, United States.
Bettina C FriesDepartment of Medicine, Infectious Disease Division, Stony Brook University, Stony Brook, New York 11794, United States.
Miklos GuttmanDepartment of Medicinal Chemistry, University of Washington, Seattle, Washington 98195, United States.ORCID 0000-0003-2419-1334

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Clyde Smith · 2020 to 2026
$43.3M
Tickborne Disease: B cell epitope discovery and mechanisms of antibody Protection75N93019C00040 · NIAID · NYSDOH/HEALTH RESEARCH, INC. · PI MANTIS, NICHOLAS J. · 2019 to 2023
$10.3M
Mechanisms of IgM mediated activation of the complement systemR01AI153191 · NIAID · UNIVERSITY OF WASHINGTON · PI GUTTMAN, MIKLOS · 2021 to 2025
$2.4M
Investigation on Replicative aging in Cryptococcus neoformans populationsR56AI127704 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI FRIES, BETTINA · 2023 to 2023
$555k
Optimization of therapeutic mAbs to carbapenem resistant Klebsiella clone ST258I01BX003741 · VA · NORTHPORT VA MEDICAL CENTER · PI FRIES, BETTINA · 2019 to 2025
–
BLRD VA I01 BX003741NIAID NIH HHS 75N93019C00040NIAID NIH HHS R01 AI153191NIAID NIH HHS R56 AI127704NIGMS NIH HHS P30 GM133894
6 · The paper itself

Abstract

Elucidating the interactions that drive antigen recognition is central to understanding antibody-mediated protection and is vital for the rational design of immunogens. Often, structural knowledge of epitopes targeted by antibodies is derived from isolated studies of monoclonal antibodies, for which numerous structural techniques exist. In contrast, there are very few approaches capable of mapping the full scope of antigen surfaces targeted by polyclonal sera through the course of a natural antibody response. Here, we develop an approach using immobilized antigen coupled to hydrogen/deuterium exchange with mass spectrometry (HDX-MS) to probe epitope targeting in the context of the fully native serum environment. Using the well-characterized

Indexed as

EnterotoxinsEpitope MappingEpitopesHydrogen Deuterium Exchange-Mass SpectrometryAnimalsenterotoxin B, staphylococcalEnterotoxinsEpitopes

Identifiers

PMID39434663
PMCPMC11583827

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.