Evidence map›Paper›PMID 27576440›Full record

ArticleRetrovirology2016

HIV-1 clade C escapes broadly neutralizing autologous antibodies with N332 glycan specificity by distinct mechanisms.

Suprit Deshpande, Shilpa Patil, Rajesh Kumar, Tandile Hermanus, Kailapuri G Murugavel, Aylur K Srikrishnan, Suniti Solomon, Lynn Morris, Jayanta Bhattacharya

Open access · goldAbstract read
In one paragraph

Article in Retrovirology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

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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

9 authors at 4 institutions in 3 countries.

Suprit DeshpandeHIV Vaccine Translational Research Laboratory, NCR Biotech Science Cluster, Translational Health Science and Technology Institute, Faridabad, Haryana, India.
Shilpa PatilHIV Vaccine Translational Research Laboratory, NCR Biotech Science Cluster, Translational Health Science and Technology Institute, Faridabad, Haryana, India.
Rajesh KumarHIV Vaccine Translational Research Laboratory, NCR Biotech Science Cluster, Translational Health Science and Technology Institute, Faridabad, Haryana, India.
Tandile HermanusNational Institute of Communicable Diseases, Johannesburg, South Africa.
Kailapuri G MurugavelYRG Care Center for AIDS Research & Education, Chennai, 600113, India.
Aylur K SrikrishnanYRG Care Center for AIDS Research & Education, Chennai, 600113, India.
Suniti SolomonYRG Care Center for AIDS Research & Education, Chennai, 600113, India.
Lynn MorrisNational Institute of Communicable Diseases, Johannesburg, South Africa.
Jayanta BhattacharyaHIV Vaccine Translational Research Laboratory, NCR Biotech Science Cluster, Translational Health Science and Technology Institute, Faridabad, Haryana, India. JBhattacharya@iavi.org.
Translational Health Science and Technology Institute · INYR Gaitonde Centre for AIDS Research and Education · INRespiratory and Meningeal Pathogens Research Unit · ZAInternational AIDS Vaccine Initiative · US

Funding

Cancer Research UKMedical Research Council U117592729Wellcome Trust 084955
6 · The paper itself

Abstract

The glycan supersite centered on N332 in the V3 base of the HIV-1 envelope (Env) is a target for broadly neutralizing antibodies (bnAbs) such as PGT121 and PGT128. In this study, we examined the basis of resistance of HIV-1 clade C Envs obtained from broadly cross neutralizing (BCN) plasma of an Indian donor with N332 specificity. Pseudotyped viruses expressing autologous envs were found to be resistant to autologous BCN plasma as well as to PGT121 and PGT128 mAbs despite the majority of Envs containing an intact N332 residue. While resistance of one of the Envs to neutralization by autologous plasma antibodies with shorter V1 loop length was found to be correlated with a N332S mutation, resistance to neutralization of rest of the Envs was found to be associated with longer V1 loop length and acquisition of protective N-glycans. In summary, we show evidence of escape of circulating HIV-1 clade C in an individual from autologous BCN antibodies by three distinct mechanisms.

Indexed as

Antibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusHIV-1HIV AntibodiesHIV Envelope Protein gp120HIV InfectionsHumansMutationNeutralization TestsPeptide FragmentsPolysaccharidesAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusHIV AntibodiesHIV Envelope Protein gp120HIV envelope protein gp120 (305-321)Peptide FragmentsPolysaccharidesEnvelopeHIV-1Neutralizing antibodyPlasma

Identifiers

PMID27576440
PMCPMC5006590
OpenAlexW2517188993

What OpenQuestion holds

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LicenceCC BY
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.