Evidence map›Paper›PMID 33370382›Full record

ArticlePLoS pathogens2020

Signal peptide of HIV-1 envelope modulates glycosylation impacting exposure of V1V2 and other epitopes.

Chitra Upadhyay, Roya Feyznezhad, Liwei Cao, Kun-Wei Chan, Kevin Liu, Weiming Yang, Hui Zhang, Jason Yolitz, James Arthos, Arthur Nadas and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Proteomic Characterization of HIV Infection.Advances in experimental medicine and biology · 2026
    Review
  7. Article
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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

13 authors at 5 institutions in 1 country.

Chitra UpadhyayIcahn School of Medicine at Mount Sinai, New York, New York, United States of America.ORCID 0000-0002-4524-1532
Roya FeyznezhadIcahn School of Medicine at Mount Sinai, New York, New York, United States of America.ORCID 0000-0002-0895-6782
Liwei CaoJohns Hopkins University, Baltimore, Maryland, United States of America.
Kun-Wei ChanDepartment of Biochemistry and Molecular Pharmacology New York University School of Medicine, New York, New York, United States of America.ORCID 0000-0001-5384-6198
Kevin LiuIcahn School of Medicine at Mount Sinai, New York, New York, United States of America.ORCID 0000-0002-0977-2694
Weiming YangJohns Hopkins University, Baltimore, Maryland, United States of America.ORCID 0000-0002-5023-2155
Hui ZhangJohns Hopkins University, Baltimore, Maryland, United States of America.ORCID 0000-0001-8726-7098
Jason YolitzLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States of America.ORCID 0000-0002-2453-6171
James ArthosLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States of America.
Arthur NadasInstitute of Environmental Medicine, New York University School of Medicine, New York, New York, United States of America.ORCID 0000-0002-6893-6759
Xiang-Peng KongDepartment of Biochemistry and Molecular Pharmacology New York University School of Medicine, New York, New York, United States of America.ORCID 0000-0001-5773-2681
Susan Zolla-PaznerIcahn School of Medicine at Mount Sinai, New York, New York, United States of America.ORCID 0000-0002-0750-2666
Catarina E HioeIcahn School of Medicine at Mount Sinai, New York, New York, United States of America.
Icahn School of Medicine at Mount Sinai · USJohns Hopkins University · USNew York University · USJames J. Peters VA Medical Center · USNational Institutes of Health · US

Funding

Structure and immunogenicity of novel trimeric HIV-1 Env immunogensR01AI145655 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI KONG, XIANGPENG · 2019 to 2023
$4.7M
Modulating antigenic and immunogenic properties of HIV Env by altering signal sequenceR01AI140909 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI UPADHYAY, CHITRA · 2019 to 2023
$3.3M
Role of signal sequence variation in governing HIV Env FunctionsR21AI124863 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI HIOE, CATARINA E, UPADHYAY, CHITRA · 2017 to 2018
$482k
Understanding Th-monocyte interactions in HIV infectionI01BX003860 · VA · JAMES J PETERS VA MEDICAL CENTER · PI HIOE, CATARINA E · 2018 to 2021
–
BLR&D Research Career Scientist Award ApplicationIK6BX004607 · VA · JAMES J PETERS VA MEDICAL CENTER · PI HIOE, CATARINA E · 2019 to 2025
–
BLRD VA I01 BX003860BLRD VA IK6 BX004607NIAID NIH HHS R01 AI140909NIAID NIH HHS R01 AI145655NIAID NIH HHS R21 AI124863
6 · The paper itself

Abstract

HIV-1 envelope (Env) is a trimer of gp120-gp41 heterodimers, synthesized from a precursor gp160 that contains an ER-targeting signal peptide (SP) at its amino-terminus. Each trimer is swathed by ~90 N-linked glycans, comprising complex-type and oligomannose-type glycans, which play an important role in determining virus sensitivity to neutralizing antibodies. We previously examined the effects of single point SP mutations on Env properties and functions. Here, we aimed to understand the impact of the SP diversity on glycosylation of virus-derived Env and virus neutralization by swapping SPs. Analyses of site-specific glycans revealed that SP swapping altered Env glycan content and occupancy on multiple N-linked glycosites, including conserved N156 and N160 glycans in the V1V2 region at the Env trimer apex and N88 at the trimer base. Virus neutralization was also affected, especially by antibodies against V1V2, V3, and gp41. Likewise, SP swaps affected the recognition of soluble and cell-associated Env by antibodies targeting distinct V1V2 configurations, V3 crown, and gp41 epitopes. These data highlight the contribution of SP sequence diversity in shaping the Env glycan content and its impact on the configuration and accessibility of V1V2 and other Env epitopes.

Indexed as

Antibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusEpitopesGlycosylationHIV-1HIV AntibodiesHumansProtein Sorting SignalsAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusEpitopesHIV AntibodiesProtein Sorting Signals

Identifiers

PMID33370382
PMCPMC7793277
OpenAlexW3115358906

What OpenQuestion holds

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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.