Evidence map›Paper›PMID 35138165›Full record

ArticleMicrobiology spectrum2022

Heat Shock Protein Member 8 (HSPA8) Is Involved in Porcine Reproductive and Respiratory Syndrome Virus Attachment and Internalization.

Lei Wang, Rui Li, Rui Geng, Longxiang Zhang, Xin-Xin Chen, Songlin Qiao, Gaiping Zhang

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 34 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

7 authors at 2 institutions in 1 country.

Lei Wang *College of Veterinary Medicine, Sichuan Agricultural University, Chengdu, Sichuan, China.
Rui Li *Key Laboratory of Animal Immunology of the Ministry of Agriculture, Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou, Henan, China.
Rui GengKey Laboratory of Animal Immunology of the Ministry of Agriculture, Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou, Henan, China.
Longxiang ZhangKey Laboratory of Animal Immunology of the Ministry of Agriculture, Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou, Henan, China.
Xin-Xin ChenKey Laboratory of Animal Immunology of the Ministry of Agriculture, Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou, Henan, China.
Songlin QiaoKey Laboratory of Animal Immunology of the Ministry of Agriculture, Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou, Henan, China.
Gaiping ZhangCollege of Veterinary Medicine, Sichuan Agricultural University, Chengdu, Sichuan, China.ORCID 0000-0002-3834-9975
Henan Academy of Agricultural Sciences · CNSichuan Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Porcine reproductive and respiratory syndrome virus (PRRSV), a porcine arterivirus, causes severe financial losses to global swine industry. Despite much research, the molecular mechanisms of PRRSV infection remains to be fully elucidated. In the current study, we uncovered the involvement of heat shock protein member 8 (HSPA8) in PRRSV attachment and internalization during infection for the first time. In detail, HSPA8 was identified to interact with PRRSV glycoprotein 4 (GP4), a major determinant for viral cellular tropism, dependent on its carboxy-terminal peptide-binding (PB) domain. Chemical inhibitors and specific small interference RNAs (siRNAs) targeting HSPA8 significantly suppressed PRRSV infection as indicated by decreased viral RNA abundance, infectivity, and titers. Especially, PRRSV attachment was inhibited by interference of its binding to HSPA8 with mouse anti-HSPA8 polyclonal antibodies (pAbs) and recombinant soluble HSPA8 protein. HSPA8 was further shown to participate in PRRSV internalization through clathrin-dependent endocytosis (CME). Collectively, these results demonstrate that HSPA8 is important for PRRSV attachment and internalization, which is a potential target to prevent and control the viral infection.

Indexed as

Virus InternalizationAnimalsAntiviral AgentsCell LineHEK293 CellsHSC70 Heat-Shock ProteinsHumansMicePorcine respiratory and reproductive syndrome virusProtein BindingReceptors, Cell SurfaceSwineViral Envelope ProteinsViral TropismAntiviral AgentsHSC70 Heat-Shock ProteinsHSPA8 protein, humanReceptors, Cell SurfaceViral Envelope ProteinsattachmentGP4HSPA8internalizationPRRSV

Identifiers

PMID35138165
PMCPMC8826899
OpenAlexW4210937070

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.