Evidence map›Paper›PMID 12072528›Full record

ArticleJournal of virology2002

The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120.

Rogier W Sanders, Miro Venturi, Linnea Schiffner, Roopa Kalyanaraman, Hermann Katinger, Kenneth O Lloyd, Peter D Kwong, John P Moore

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 317 papers.

0numbers the graph read from it
0cells of the map it votes in
317citing papers in PubMed
9.1field-weighted citation impact, top 1% of its field
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

317 citing papers in PubMed, 547 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. ACS central science · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

257 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 2 countries.

Rogier W SandersDept. of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA.
Miro Venturi
Linnea Schiffner
Roopa Kalyanaraman
Hermann Katinger
Kenneth O Lloyd
Peter D Kwong
John P Moore
Cornell University · USUniversity of Amsterdam · NLNational Institute of Allergy and Infectious Diseases · USNational Institutes of Health · US

Funding

NEUTRALIZATION OF PRIMARY HIV1 VIRUSESR37AI036082 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOORE, JOHN P · 1998 to 2017
$7.0M
Neutralization of Primate Immunodeficiency VirusesR01AI036082 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI JOHN P MOORE · 1994 to 2026
$4.3M
MODIFIED ENVELOPE GLYCOPROTEINS FOR HIV1 VACCINER01AI045463 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOORE, JOHN P · 1999 to 2010
$4.2M
TOPOLOGICAL ANALYSIS OF HIV-1 ENVELOPE GLYCOPROTEINSR01AI039420 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1996 to 2004
$1.6M
Neutralization Mechanisms Of HIV-1 Monoclonal AntibodiesZ01AI005022 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI KWONG, PETER D · 2002 to 2008
$733k
NIAID NIH HHS AI36082NIAID NIH HHS AI39420NIAID NIH HHS AI45463NIAID NIH HHS R01 AI036082NIAID NIH HHS R01 AI039420NIAID NIH HHS R01 AI045463NIAID NIH HHS R37 AI036082
6 · The paper itself

Abstract

We have analyzed the unique epitope for the broadly neutralizing human monoclonal antibody (MAb) 2G12 on the gp120 surface glycoprotein of human immunodeficiency virus type 1 (HIV-1). Sequence analysis, focusing on the conservation of relevant residues across multiple HIV-1 isolates, refined the epitope that was defined previously by substitutional mutagenesis (A. Trkola, M. Purtscher, T. Muster, C. Ballaun, A. Buchacher, N. Sullivan, K. Srinivasan, J. Sodroski, J. P. Moore, and H. Katinger, J. Virol. 70:1100-1108, 1996). In a biochemical study, we digested recombinant gp120 with various glycosidase enzymes of known specificities and showed that the 2G12 epitope is lost when gp120 is treated with mannosidases. Computational analyses were used to position the epitope in the context of the virion-associated envelope glycoprotein complex, to determine the variability of the surrounding surface, and to calculate the surface accessibility of possible glycan- and polypeptide-epitope components. Together, these analyses suggest that the 2G12 epitope is centered on the high-mannose and/or hybrid glycans of residues 295, 332, and 392, with peripheral glycans from 386 and 448 on either flank. The epitope is mannose dependent and composed primarily of carbohydrate, with probably no direct involvement of the gp120 polypeptide surface. It resides on a face orthogonal to the CD4 binding face, on a surface proximal to, but distinct from, that implicated in coreceptor binding. Its conservation amidst an otherwise highly variable gp120 surface suggests a functional role for the 2G12 binding site, perhaps related to the mannose-dependent attachment of HIV-1 to DC-SIGN or related lectins that facilitate virus entry into susceptible target cells.

Indexed as

Epitope MappingAntibodies, MonoclonalCarbohydrate SequenceGlycoside HydrolasesGlycosylationHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansMannoseModels, MolecularMolecular Sequence DataNeutralization TestsSequence Analysis, DNAAntibodies, MonoclonalGlycoside HydrolasesHIV AntibodiesHIV Envelope Protein gp120Mannose

Identifiers

PMID12072528
PMCPMC136300
OpenAlexW2163558461

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.