Evidence map›Paper›PMID 14722307›Full record

ArticleJournal of virology2004

Removal of N-linked glycosylation sites in the V1 region of simian immunodeficiency virus gp120 results in redirection of B-cell responses to V3.

Kelly Stefano Cole, Jonathan D Steckbeck, Jennifer L Rowles, Ronald C Desrosiers, Ronald C Montelaro

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

40 citing papers in PubMed, 67 citations in OpenAlex.

  1. ExploringFrontiers in immunology · 2022
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Functional contributions of carbohydrate on AIDS virus glycoprotein.The Yale journal of biology and medicine · 2010
    Review
  19. Article
  20. 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

5 authors at 2 institutions in 2 countries.

Kelly Stefano ColeDepartment of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, USA. stefcole@pitt.edu
Jonathan D Steckbeck
Jennifer L Rowles
Ronald C Desrosiers
Ronald C Montelaro
Harvard University · USUniversity of Pittsburgh · US

Funding

DOMAIN-SPECIFIC SEROLOGY FOR SIV/SHIV VACCINE EVALUATIONR01AI047758 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MONTELARO, RONALD C · 2000 to 2004
$1.3M
DEVELOPMENT OF AN AIDS PROTOTYPE VACCINE USING SIVU01AI028243 · NIAID · TULANE UNIVERSITY OF LOUISIANA · PI MURPHEY-CORB, MICHAEL A · 1989 to 1993
–
RHESUS MONOCLONAL ANTIBODIES TO SIV GLYCOPROTEINSU19AI028243 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MURPHEY-CORB, MICHAEL A · 1995 to 1997
–
NIAID NIH HHS AI-28243NIAID NIH HHS AI-47758NIAID NIH HHS R01 AI047758
6 · The paper itself

Abstract

One mechanism of immune evasion utilized by human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) envelope glycoproteins is the presence of a dense carbohydrate shield. Accumulating evidence from in vitro and in vivo experiments suggests that alterations in N-linked glycosylation of SIV gp120 can enhance host humoral immune responses that may be involved in immune control. The present study was designed to determine the ability of glycosylation mutant viruses to redirect antibody responses to shielded envelope epitopes. The influence of glycosylation on the maturation and specificity of antibody responses elicited by glycosylation mutant viruses containing mutations of specific N-linked sites in and near the V1 and V2 regions of SIVmac239 gp120 was determined. Results from these studies demonstrated a remarkably similar maturation of antibody responses to native, fully glycosylated envelope proteins. However, analyses of antibodies to defined envelope domains revealed that mutation of glycosylation sites in V1 resulted in increased antibody recognition to epitopes in V1. In addition, we demonstrated for the first time that mutation of glycosylation sites in V1 resulted in a redirection of antibody responses to the V3 loop. Taken together, these results demonstrate that N-linked glycosylation is a determinant of SIV envelope B-cell immunogenicity in addition to in vitro antigenicity. In addition, our results demonstrate that the absence of N-linked carbohydrates at specific sites can influence the exposure of epitopes quite distant in the linear sequence.

Indexed as

MutationAmino Acid SequenceAnimalsAntibodies, ViralAntibody AffinityB-LymphocytesGlycosylationHIV Envelope Protein gp120HumansMacaca mulattaMembrane GlycoproteinsMolecular Sequence DataPeptide FragmentsProtein ConformationRecombinant Fusion ProteinsSimian Immunodeficiency VirusAntibodies, Viralgp120 protein, Simian immunodeficiency virusHIV Envelope Protein gp120HIV envelope protein gp120 (305-321)Membrane GlycoproteinsPeptide FragmentsRecombinant Fusion ProteinsViral Envelope Proteins

Identifiers

PMID14722307
PMCPMC321372
OpenAlexW2165415478

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.