Evidence map›Paper›PMID 31024744›Full record

ArticleActa naturae

Consensus Integrase of a New HIV-1 Genetic Variant CRF63_02A1.

Y Y Agapkina, M A Pustovarova, S P Korolev, D P Zyryanova, V V Ivlev, A V Totmenin, N M Gashnikova, M B Gottikh

Open access · diamondAbstract read
PubMed Full text at PMC
In one paragraph

Article in Acta naturae. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 95% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

8 authors at 3 institutions in 2 countries.

Y Y AgapkinaLomonosov Moscow State University, Chemistry Department and Belozersky Institute of Physical Chemical Biology, Leninskie gory 1/40, 119991, Moscow, Russia.
M A PustovarovaLomonosov Moscow State University, Chemistry Department and Belozersky Institute of Physical Chemical Biology, Leninskie gory 1/40, 119991, Moscow, Russia.
S P KorolevLomonosov Moscow State University, Chemistry Department and Belozersky Institute of Physical Chemical Biology, Leninskie gory 1/40, 119991, Moscow, Russia.
D P ZyryanovaState Research Center of Virology and Biotechnology "Vector", 630559, Koltsovo, Russia.
V V IvlevState Research Center of Virology and Biotechnology "Vector", 630559, Koltsovo, Russia.
A V TotmeninState Research Center of Virology and Biotechnology "Vector", 630559, Koltsovo, Russia.
N M GashnikovaState Research Center of Virology and Biotechnology "Vector", 630559, Koltsovo, Russia.
M B GottikhLomonosov Moscow State University, Chemistry Department and Belozersky Institute of Physical Chemical Biology, Leninskie gory 1/40, 119991, Moscow, Russia.
State Research Center of Virology and Biotechnology VECTOR · RULomonosov Moscow State University · RUPhysico-Technical Institute · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The high genetic variability of the human immunodeficiency virus (HIV-1) leads to a constant emergence of new genetic variants, including the recombinant virus CRF63_02A1, which is widespread in the Siberian Federal District of Russia. We studied HIV-1 CRF63_02A1 integrase (IN_CRF) catalyzing the incorporation of viral DNA into the genome of an infected cell. The consensus sequence was designed, recombinant integrase was obtained, and its DNA-binding and catalytic activities were characterized. The stability of the IN_CRF complex with the DNA substrate did not differ from the complex stability for subtype A and B integrases; however, the rate of complex formation was significantly higher. The rates and efficiencies of 3'-processing and strand transfer reactions catalyzed by IN_CRF were found to be higher, too. Apparently, all these distinctive features of IN_CRF may result from specific amino acid substitutions in its N-terminal domain, which plays an important role in enzyme multimerization and binding to the DNA substrate. It was also found that the drug resistance mutations Q148K/G140S and G118R/E138K significantly reduce the catalytic activity of IN_CRF and its sensitivity to the strand transfer inhibitor raltegravir. Reduction in sensitivity to raltegravir was found to be much stronger in the case of double-mutation Q148K/G140S.

Indexed as

CRF63_02A1 genetic variantdrug resistance mutationshuman immunodeficiency virusintegrasestrand transfer inhibitor

Identifiers

PMID31024744
PMCPMC6475865
OpenAlexW2944960986

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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.