Article(id=1238813317993656611, tenantId=1146029695717560320, journalId=1192105938417971205, issueId=1238813307784712441, articleNumber=null, orderNo=null, doi=10.13343/j.cnki.wsxb.20250714, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=research-article, receivedDate=1758211200000, receivedDateStr=2025-09-19, revisedDate=null, revisedDateStr=null, acceptedDate=1764604800000, acceptedDateStr=2025-12-02, onlineDate=1773285711047, onlineDateStr=2026-03-12, pubDate=1772553600000, pubDateStr=2026-03-04, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1773285711047, onlineIssueDateStr=2026-03-12, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1773285711047, creator=13701087609, updateTime=1773285711047, updator=13701087609, issue=Issue{id=1238813307784712441, tenantId=1146029695717560320, journalId=1192105938417971205, year='2026', volume='66', issue='3', pageStart='961', pageEnd='1466', issueExtLink='null', onlineDate='null', pubDate='null', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=-1, specialIssue=null, createTime=1773285708614, creator=13701087609, updateTime=1773291912509, updator=13701087609, preIssue=null, nextIssue=null, ext={EN=IssueExt(id=1238839328915378858, tenantId=1146029695717560320, journalId=1192105938417971205, issueId=1238813307784712441, language=EN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=), CN=IssueExt(id=1238839328915378859, tenantId=1146029695717560320, journalId=1192105938417971205, issueId=1238813307784712441, language=CN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=)}, issueFiles=null}, startPage=990, endPage=1006, ext={EN=ArticleExt(id=1238813318484390201, articleId=1238813317993656611, tenantId=1146029695717560320, journalId=1192105938417971205, language=EN, title=Research progress on the impact of heat shock protein family A member 8 on virus infection of host cells, columnId=1192149543727808575, journalTitle=Acta Microbiologica Sinica, columnName=Review, runingTitle=null, highlight=null, articleAbstract=

Heat shock protein family A member 8 (HSPA8) is a widely distributed molecular chaperone in cells. HSPA8 is involved in multiple cellular physiological processes, mainly including the correct folding and transport of proteins, stress responses, presentation of antigenic proteins, mediation of autophagy, and immune regulation. It is also crucial for maintaining the homeostasis of the intracellular environment. In addition, HSPA8 plays a key role in multiple processes of virus infections. This paper reviewed the important roles and molecular mechanisms of HSPA8 in processes such as virus adhesion, formation of virus glycoprotein-receptor complexes, internalization, uncoating, genome replication, assembly, and regulation of host metabolism and immune responses, with the hope of laying a foundation for the subsequent development of drugs targeting HSPA8 for the treatment of virus infections.

, correspAuthors=Weike LI, Jiansheng ZHOU, authorNote=null, correspAuthorsNote=, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=null, pdfFileSize=null, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=null, mapNumber=null, authorCompany=null, fund=null, authors=null, authorsList=Siyuan LI, Zhentao ZHANG, Yanlong LIN, Fei WANG, Xiaobo HE, Jianshe YANG, Weike LI, Jiansheng ZHOU), CN=ArticleExt(id=1238813319465857389, articleId=1238813317993656611, tenantId=1146029695717560320, journalId=1192105938417971205, language=CN, title=热休克蛋白8影响病毒感染宿主细胞的研究进展, columnId=1192149543882997826, journalTitle=微生物学报, columnName=综述, runingTitle=null, highlight=null, articleAbstract=

热休克蛋白8 (heat shock protein family A member 8, HSPA8)是一种广泛存在于细胞内的分子伴侣蛋白。该蛋白参与多项细胞生理过程，主要包括蛋白质的正确折叠与转运、应激反应、抗原蛋白呈递、自噬介导以及免疫调控等，对维持细胞内环境稳态至关重要。此外，HSPA8在病毒感染的多个过程中发挥关键作用。本文综述了HSPA8在病毒黏附、病毒糖蛋白-受体复合物形成、内化、脱壳、基因组复制、组装，以及调节宿主代谢和免疫反应等过程中所发挥的重要作用及其分子机制，为后续靶向HSPA8的抗病毒药物研发奠定了基础。

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articleId=1238813317993656611, language=EN, label=Figure 1, caption=HSPA8 homology analysis and structural schematic diagram. A: Phylogenetic tree of HSPA8; B: Percentage identity matrix of HSPA8; C: Schematic diagram of the domains of HSPA8; D: Schematic diagram of the higher-order structure of HSPA8 (UniProt: P11142; PDB ID: 3AGY)., figureFileSmall=I0ZOAzj8KnlcgqHoJoFibw==, figureFileBig=xyRnESX+io/f1HNNOkX23Q==, tableContent=null), ArticleFig(id=1238904045830722145, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813317993656611, language=CN, label=图1, caption=HSPA8同源性分析和结构示意图。A：HSPA8系统发育树；B：HSPA8百分比一致性矩阵；C：HSPA8的结构域示意图；D：HSPA8的高级结构示意图(UniProt：P11142；PDB ID：3AGY)。, figureFileSmall=I0ZOAzj8KnlcgqHoJoFibw==, figureFileBig=xyRnESX+io/f1HNNOkX23Q==, tableContent=null), ArticleFig(id=1238904045918802531, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813317993656611, language=EN, label=Figure 2, caption=HSPA8 affects the virus’s infection of host cells. A: HSPA8 regulates host metabolism (Such as HCV, can induce the expression of HNF-1α through NS5A. HSPA8 can selectively bind to HNF-1α and deliver it to Lamp 2A on the surface of lysosomes, promoting the degradation of HNF-1α through the CMA pathway, and then inhibiting the expression of the GLUT2 gene to suppress the cell’s uptake of glucose); B: HSPA8 regulates the host immune pathway [DNA-PK recognizes foreign viral DNA and is activated, regulating the phosphorylation of HSPA8 at Ser 638 and transmitting signals. Phosphorylated HSPA8 interacts with co-chaperone proteins, such as TF, and participates in the regulation of the expression of downstream antiviral genes]; C: HSPA8 is involved in the infection of host cells by viruses., figureFileSmall=Ld3VC1fPbCQHcmPVG3Z9FQ==, figureFileBig=HkM0RnHnIHcm0/MrxdGjoQ==, tableContent=null), ArticleFig(id=1238904046032048741, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813317993656611, language=CN, label=图2, caption=HSPA8影响病毒感染宿主细胞。A：HSPA8调节宿主代谢(以HCV为例，HCV可通过NS5A诱导表达HNF-1α，HSPA8可以选择性结合HNF-1α，并将其递送至溶酶体表面的Lamp 2A，促进HNF-1α通过CMA途径降解，进而抑制GLUT2基因表达来抑制细胞对葡萄糖的摄取)；B：HSPA8调节宿主免疫通路[DNA-PK识别外源病毒DNA并激活，调控HSPA8的Ser 638位磷酸化并传递信号，磷酸化的HSPA8与共伴侣蛋白，如转录因子(transcription factor, TF)相互作用，参与下游抗病毒基因的表达调控]；C：HSPA8参与病毒感染宿主细胞。, figureFileSmall=Ld3VC1fPbCQHcmPVG3Z9FQ==, figureFileBig=HkM0RnHnIHcm0/MrxdGjoQ==, tableContent=null), ArticleFig(id=1238904046090768999, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813317993656611, language=EN, label=Figure 3, caption=Antiviral strategies of HSPA8. A: Small molecule inhibitors of HSPA8, such as halofuginone, can inhibit its ATP-binding domain; B: RNA interference technology targeting HSPA8, such as siRNA, can degrade the mRNA of HSPA8; C: Antibodies targeting HSPA8; D: Natural compounds that inhibit HSPA8, such as pristimerin, can induce the degradation of HSPA8., figureFileSmall=AsZ6ofizK0zbAFujugQkRg==, figureFileBig=f1UdquA7E1pxVUzNRQyfAw==, tableContent=null), ArticleFig(id=1238904046153683561, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813317993656611, language=CN, label=图3, caption=靶向HSPA8的抗病毒策略。A：HSPA8小分子抑制剂，如卤夫酮(halofuginone)可以抑制其ATP结合结构域；B：针对HSPA8的RNA干扰技术，如siRNA可以降解HSPA8的mRNA；C：靶向HSPA8抗体；D：抑制HSPA8的天然化合物，如扁塑藤素(pristimerin)可以诱导机体降解HSPA8。, figureFileSmall=AsZ6ofizK0zbAFujugQkRg==, figureFileBig=f1UdquA7E1pxVUzNRQyfAw==, tableContent=null), ArticleFig(id=1238904046212403818, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813317993656611, language=EN, label=Table 1, caption=

The role of HSPA8 in different viral infections

, figureFileSmall=null, figureFileBig=null, tableContent=

病毒感染阶段 Stages of viral infection	病毒 Virus	HSPA8定位 HSPA8 location	作用机制 Mechanism of action	参考文献 References
Attachment	IBV	Cellular membrane	HSPA8 is the additional attachment factor	[31]
	PRRSV		HSPA8 and CD163 are involved in the formation of the viral receptor complex	[34]
	RGNNV		HSPA8 and MmHSP90ab1 are involved in the formation of the viral receptor complex	[37]
Penetration	TGEV	Cellular membrane, cytoplasm	HSPA8 directs virus internalization via CME	[41]
	JEV		HSPA8 directs virus internalization via CME	[43]
	Rotavirus		HSPA8 induces conformational changes in viral particles to facilitate viral entry	[45]
Uncoating	ASFV	Cytoplasm	HSPA8 promotes viral uncoating by degrading the viral capsid protein via autophagy	[49]
	IAV		HSPA8 promotes the release of the genome after viral uncoating and the subsequent transport of the viral ribonucleoprotein complex	[52]
Replication	EBOV	Cytoplasm, nucleus	HSPA8 binds to the trailing region of EBOV	[57]
	RABV		HSPA8 binds to the leRNA of RABV	[59]
	DENV		The interaction between dvNS3 and HSPA8 disrupts the formation of the RISC by displacing TRBP	[61]
	MVC		HSPA8 translocates NS1 or VP2 proteins to the nucleus	[63]
Assembly	HPV	PML	HSPA8 assists L2 in integrating into L1 and then dissociates upon completion of viral assembly	[66]
	CNV	Cytoplasm	HSPA8 binds to CP, maintains its solubility, and directly promotes VLP assembly	[68]

), ArticleFig(id=1238904047659438700, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1238813317993656611, language=CN, label=表1, caption=

HSPA8在不同病毒感染中的作用

, figureFileSmall=null, figureFileBig=null, tableContent=

病毒感染阶段 Stages of viral infection	病毒 Virus	HSPA8定位 HSPA8 location	作用机制 Mechanism of action	参考文献 References
Attachment	IBV	Cellular membrane	HSPA8 is the additional attachment factor	[31]
	PRRSV		HSPA8 and CD163 are involved in the formation of the viral receptor complex	[34]
	RGNNV		HSPA8 and MmHSP90ab1 are involved in the formation of the viral receptor complex	[37]
Penetration	TGEV	Cellular membrane, cytoplasm	HSPA8 directs virus internalization via CME	[41]
	JEV		HSPA8 directs virus internalization via CME	[43]
	Rotavirus		HSPA8 induces conformational changes in viral particles to facilitate viral entry	[45]
Uncoating	ASFV	Cytoplasm	HSPA8 promotes viral uncoating by degrading the viral capsid protein via autophagy	[49]
	IAV		HSPA8 promotes the release of the genome after viral uncoating and the subsequent transport of the viral ribonucleoprotein complex	[52]
Replication	EBOV	Cytoplasm, nucleus	HSPA8 binds to the trailing region of EBOV	[57]
	RABV		HSPA8 binds to the leRNA of RABV	[59]
	DENV		The interaction between dvNS3 and HSPA8 disrupts the formation of the RISC by displacing TRBP	[61]
	MVC		HSPA8 translocates NS1 or VP2 proteins to the nucleus	[63]
Assembly	HPV	PML	HSPA8 assists L2 in integrating into L1 and then dissociates upon completion of viral assembly	[66]
	CNV	Cytoplasm	HSPA8 binds to CP, maintains its solubility, and directly promotes VLP assembly	[68]

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