Human membrane protein Tim-3 facilitates hepatitis A virus entry into target cells
In this study, a cellular surface membrane protein of immunoglobulin (Ig) superfamily (IgSF) was identified from a human dendritic cell (DC) cDNA library by large-scale random sequencing, which is identical to previously reported Tim-3 (T-cell Ig- and mucin-domain-containing molecule 3). Recent data...
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| Veröffentlicht in: | International journal of molecular medicine 2006-06, Vol.17 (6), p.1093-1099 |
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| container_title | International journal of molecular medicine |
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| creator | Sui, Lili Li, Nan Zhang, Wenyuan Chen, Yong Zheng, Yuanyuan Wan, Tao Zhang, Weiping Yang, Yadong Fang, Guojian Mao, Jiangsen Cao, Xuetao |
| description | In this study, a cellular surface membrane protein of immunoglobulin (Ig)
superfamily (IgSF) was identified from a human dendritic cell (DC) cDNA library
by large-scale random sequencing, which is identical to previously reported Tim-3
(T-cell Ig- and mucin-domain-containing molecule 3). Recent data have suggested
the association of the 281-residue mouse Tim-3 molecule with Th1-related T cell
responses and disease in mice. Human Tim-3 is a 301-residue type I membrane protein
whose extracellular region contains a Cys-rich Ig-like domain and a mucin domain,
the characteristics of Tim proteins. It shows significant homology to human hepatitis
A virus (HAV) cellular receptor-1 (HuHAVcr-1)/Tim-1. Human Tim-3 mRNA was highly
expressed in monocytes or monocyte-derived cells, and the expression level decreased
when DC underwent maturation and activation. There is no previous report on the
biological functions of human Tim-3, especially the involvement in virus infection.
We demonstrated that HeLa cells, which are refractory to HAV infection, acquired
a limited susceptibility to HAV infection after stably overexpressing human Tim-3
as confirmed by Western blot analysis using anti-Tim-3 antibody, but Tim-3-Fc
fusion protein had no direct HAV-binding activity. The results indicated that
human Tim-3 can promote HAV entry into target cells but itself may not function
as a cellular receptor of HAV. |
| doi_str_mv | 10.3892/ijmm.17.6.1093 |
| format | Article |
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superfamily (IgSF) was identified from a human dendritic cell (DC) cDNA library
by large-scale random sequencing, which is identical to previously reported Tim-3
(T-cell Ig- and mucin-domain-containing molecule 3). Recent data have suggested
the association of the 281-residue mouse Tim-3 molecule with Th1-related T cell
responses and disease in mice. Human Tim-3 is a 301-residue type I membrane protein
whose extracellular region contains a Cys-rich Ig-like domain and a mucin domain,
the characteristics of Tim proteins. It shows significant homology to human hepatitis
A virus (HAV) cellular receptor-1 (HuHAVcr-1)/Tim-1. Human Tim-3 mRNA was highly
expressed in monocytes or monocyte-derived cells, and the expression level decreased
when DC underwent maturation and activation. There is no previous report on the
biological functions of human Tim-3, especially the involvement in virus infection.
We demonstrated that HeLa cells, which are refractory to HAV infection, acquired
a limited susceptibility to HAV infection after stably overexpressing human Tim-3
as confirmed by Western blot analysis using anti-Tim-3 antibody, but Tim-3-Fc
fusion protein had no direct HAV-binding activity. The results indicated that
human Tim-3 can promote HAV entry into target cells but itself may not function
as a cellular receptor of HAV.</description><identifier>ISSN: 1107-3756</identifier><identifier>EISSN: 1791-244X</identifier><identifier>DOI: 10.3892/ijmm.17.6.1093</identifier><identifier>PMID: 16685421</identifier><language>eng</language><publisher>Greece: D.A. Spandidos</publisher><subject>Amino Acid Sequence ; Dendritic Cells - metabolism ; HeLa Cells ; Hepatitis A - metabolism ; Hepatitis A - virology ; Hepatitis A virus - physiology ; Hepatitis A Virus Cellular Receptor 2 ; Humans ; Immunoglobulin Fc Fragments - genetics ; Immunoglobulin Fc Fragments - metabolism ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Molecular Sequence Data ; Monocytes - metabolism ; Receptors, Virus - chemistry ; Receptors, Virus - genetics ; Receptors, Virus - metabolism ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; RNA, Messenger - metabolism ; Sequence Alignment ; Transfection</subject><ispartof>International journal of molecular medicine, 2006-06, Vol.17 (6), p.1093-1099</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c371t-f32e758d8ce2cb5d3b3e14aa6360cd630c94c784f8e9c0a7a9135a406ff763d53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,5571,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16685421$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sui, Lili</creatorcontrib><creatorcontrib>Li, Nan</creatorcontrib><creatorcontrib>Zhang, Wenyuan</creatorcontrib><creatorcontrib>Chen, Yong</creatorcontrib><creatorcontrib>Zheng, Yuanyuan</creatorcontrib><creatorcontrib>Wan, Tao</creatorcontrib><creatorcontrib>Zhang, Weiping</creatorcontrib><creatorcontrib>Yang, Yadong</creatorcontrib><creatorcontrib>Fang, Guojian</creatorcontrib><creatorcontrib>Mao, Jiangsen</creatorcontrib><creatorcontrib>Cao, Xuetao</creatorcontrib><title>Human membrane protein Tim-3 facilitates hepatitis A virus entry into target cells</title><title>International journal of molecular medicine</title><addtitle>Int J Mol Med</addtitle><description>In this study, a cellular surface membrane protein of immunoglobulin (Ig)
superfamily (IgSF) was identified from a human dendritic cell (DC) cDNA library
by large-scale random sequencing, which is identical to previously reported Tim-3
(T-cell Ig- and mucin-domain-containing molecule 3). Recent data have suggested
the association of the 281-residue mouse Tim-3 molecule with Th1-related T cell
responses and disease in mice. Human Tim-3 is a 301-residue type I membrane protein
whose extracellular region contains a Cys-rich Ig-like domain and a mucin domain,
the characteristics of Tim proteins. It shows significant homology to human hepatitis
A virus (HAV) cellular receptor-1 (HuHAVcr-1)/Tim-1. Human Tim-3 mRNA was highly
expressed in monocytes or monocyte-derived cells, and the expression level decreased
when DC underwent maturation and activation. There is no previous report on the
biological functions of human Tim-3, especially the involvement in virus infection.
We demonstrated that HeLa cells, which are refractory to HAV infection, acquired
a limited susceptibility to HAV infection after stably overexpressing human Tim-3
as confirmed by Western blot analysis using anti-Tim-3 antibody, but Tim-3-Fc
fusion protein had no direct HAV-binding activity. The results indicated that
human Tim-3 can promote HAV entry into target cells but itself may not function
as a cellular receptor of HAV.</description><subject>Amino Acid Sequence</subject><subject>Dendritic Cells - metabolism</subject><subject>HeLa Cells</subject><subject>Hepatitis A - metabolism</subject><subject>Hepatitis A - virology</subject><subject>Hepatitis A virus - physiology</subject><subject>Hepatitis A Virus Cellular Receptor 2</subject><subject>Humans</subject><subject>Immunoglobulin Fc Fragments - genetics</subject><subject>Immunoglobulin Fc Fragments - metabolism</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Monocytes - metabolism</subject><subject>Receptors, Virus - chemistry</subject><subject>Receptors, Virus - genetics</subject><subject>Receptors, Virus - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Alignment</subject><subject>Transfection</subject><issn>1107-3756</issn><issn>1791-244X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkM9LwzAUx4Mobk6vHiUnb61J86s5jqFOGAgywVtI01QzmnYmqbD_3pZNPDzeO3zel_c-ANxilJNSFg9u532ORc5zjCQ5A3MsJM4KSj_OxxkjkRHB-AxcxbhDqGBUlpdghjkvGS3wHLytB6876K2vgu4s3Ic-WdfBrfMZgY02rnVJJxvhl93r5JKLcAl_XBgitF0KB-i61MOkw6dN0Ni2jdfgotFttDenvgDvT4_b1TrbvD6_rJabzBCBU9aQwgpW1qWxhalYTSpiMdWaE45MzQkykhpR0qa00iAttMSEaYp40whOakYW4P6YO978PdiYlHdxumD8ox-i4kKygmEygvkRNKGPMdhG7YPzOhwURmqyqCaLCgvF1WRxXLg7JQ-Vt_U_ftI2AtkRiHvd1a7u4z_z5xwLPoWNJckvs1J8bw</recordid><startdate>20060601</startdate><enddate>20060601</enddate><creator>Sui, Lili</creator><creator>Li, Nan</creator><creator>Zhang, Wenyuan</creator><creator>Chen, Yong</creator><creator>Zheng, Yuanyuan</creator><creator>Wan, Tao</creator><creator>Zhang, Weiping</creator><creator>Yang, Yadong</creator><creator>Fang, Guojian</creator><creator>Mao, Jiangsen</creator><creator>Cao, Xuetao</creator><general>D.A. Spandidos</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20060601</creationdate><title>Human membrane protein Tim-3 facilitates hepatitis A virus entry into target cells</title><author>Sui, Lili ; Li, Nan ; Zhang, Wenyuan ; Chen, Yong ; Zheng, Yuanyuan ; Wan, Tao ; Zhang, Weiping ; Yang, Yadong ; Fang, Guojian ; Mao, Jiangsen ; Cao, Xuetao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c371t-f32e758d8ce2cb5d3b3e14aa6360cd630c94c784f8e9c0a7a9135a406ff763d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Dendritic Cells - metabolism</topic><topic>HeLa Cells</topic><topic>Hepatitis A - metabolism</topic><topic>Hepatitis A - virology</topic><topic>Hepatitis A virus - physiology</topic><topic>Hepatitis A Virus Cellular Receptor 2</topic><topic>Humans</topic><topic>Immunoglobulin Fc Fragments - genetics</topic><topic>Immunoglobulin Fc Fragments - metabolism</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Monocytes - metabolism</topic><topic>Receptors, Virus - chemistry</topic><topic>Receptors, Virus - genetics</topic><topic>Receptors, Virus - metabolism</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Alignment</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sui, Lili</creatorcontrib><creatorcontrib>Li, Nan</creatorcontrib><creatorcontrib>Zhang, Wenyuan</creatorcontrib><creatorcontrib>Chen, Yong</creatorcontrib><creatorcontrib>Zheng, Yuanyuan</creatorcontrib><creatorcontrib>Wan, Tao</creatorcontrib><creatorcontrib>Zhang, Weiping</creatorcontrib><creatorcontrib>Yang, Yadong</creatorcontrib><creatorcontrib>Fang, Guojian</creatorcontrib><creatorcontrib>Mao, Jiangsen</creatorcontrib><creatorcontrib>Cao, Xuetao</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of molecular medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sui, Lili</au><au>Li, Nan</au><au>Zhang, Wenyuan</au><au>Chen, Yong</au><au>Zheng, Yuanyuan</au><au>Wan, Tao</au><au>Zhang, Weiping</au><au>Yang, Yadong</au><au>Fang, Guojian</au><au>Mao, Jiangsen</au><au>Cao, Xuetao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human membrane protein Tim-3 facilitates hepatitis A virus entry into target cells</atitle><jtitle>International journal of molecular medicine</jtitle><addtitle>Int J Mol Med</addtitle><date>2006-06-01</date><risdate>2006</risdate><volume>17</volume><issue>6</issue><spage>1093</spage><epage>1099</epage><pages>1093-1099</pages><issn>1107-3756</issn><eissn>1791-244X</eissn><abstract>In this study, a cellular surface membrane protein of immunoglobulin (Ig)
superfamily (IgSF) was identified from a human dendritic cell (DC) cDNA library
by large-scale random sequencing, which is identical to previously reported Tim-3
(T-cell Ig- and mucin-domain-containing molecule 3). Recent data have suggested
the association of the 281-residue mouse Tim-3 molecule with Th1-related T cell
responses and disease in mice. Human Tim-3 is a 301-residue type I membrane protein
whose extracellular region contains a Cys-rich Ig-like domain and a mucin domain,
the characteristics of Tim proteins. It shows significant homology to human hepatitis
A virus (HAV) cellular receptor-1 (HuHAVcr-1)/Tim-1. Human Tim-3 mRNA was highly
expressed in monocytes or monocyte-derived cells, and the expression level decreased
when DC underwent maturation and activation. There is no previous report on the
biological functions of human Tim-3, especially the involvement in virus infection.
We demonstrated that HeLa cells, which are refractory to HAV infection, acquired
a limited susceptibility to HAV infection after stably overexpressing human Tim-3
as confirmed by Western blot analysis using anti-Tim-3 antibody, but Tim-3-Fc
fusion protein had no direct HAV-binding activity. The results indicated that
human Tim-3 can promote HAV entry into target cells but itself may not function
as a cellular receptor of HAV.</abstract><cop>Greece</cop><pub>D.A. Spandidos</pub><pmid>16685421</pmid><doi>10.3892/ijmm.17.6.1093</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | International journal of molecular medicine, 2006-06, Vol.17 (6), p.1093-1099 |
| issn | 1107-3756 1791-244X |
| language | eng |
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| source | Spandidos Publications Journals; MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Dendritic Cells - metabolism HeLa Cells Hepatitis A - metabolism Hepatitis A - virology Hepatitis A virus - physiology Hepatitis A Virus Cellular Receptor 2 Humans Immunoglobulin Fc Fragments - genetics Immunoglobulin Fc Fragments - metabolism Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Molecular Sequence Data Monocytes - metabolism Receptors, Virus - chemistry Receptors, Virus - genetics Receptors, Virus - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism RNA, Messenger - metabolism Sequence Alignment Transfection |
| title | Human membrane protein Tim-3 facilitates hepatitis A virus entry into target cells |
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