TYMSTR, a putative chemokine receptor selectively expressed in activated T cells, exhibits HIV-1 coreceptor function

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1997
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Loetscher, Marcel
Amara, Ali
Oberlin, Estelle
Brass, Nicole
Loetscher, Pius
D'Apuzzo, Massimo
Meese, Eckart
Rousset, Dominique
Moser, Bernhard
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Current Biology. 1997, 7(9), pp. 652-660. ISSN 0960-9822. eISSN 1879-0445. Available under: doi: 10.1016/S0960-9822(06)00292-2
Zusammenfassung

Background: Chemokines bind to specific receptors and mediate leukocyte migration to sites of inflammation. Recently, some chemokine receptors, notably CXCR4 and CCR5, have been shown to be essential fusion factors on target cells for infection by human immunodeficiency virus (HIV); the chemokines bound by these receptors have also been shown to act as potent inhibitors of HIV infection. Here, we describe the isolation of a novel, putative chemokine receptor.

Results: We have isolated the cDNA for a putative human chemokine receptor, which we have termed TYMSTR (T-lymphocyte-expressed seven-transmembrane domain receptor). The TYMSTR gene is localized to human chromosome 3 and encodes a protein that has a high level of identity with chemokine receptors. TYMSTR mRNA was selectively expressed in interleukin-2-stimulated T lymphocytes but not in freshly isolated lymphocytes and leukocytes or related cell lines. The natural ligand for TYMSTR was not identified among 32 human chemokines and other potential ligands. Cells co-expressing TYMSTR and human CD4 fused with cells expressing envelope glycoproteins of macrophage (M)-tropic HIV-1 as well as T-cell line (T)-tropic HIV-1 isolates. Addition of infectious, T-tropic HIV-1 particles to TYMSTR/CD4-expressing cells resulted in viral entry and proviral DNA formation.

Conclusions: Our findings demonstrate that TYMSTR, in combination with CD4, mediates HIV-1 fusion and entry. The high-level expression of TYMSTR in CD4+ T lymphocytes and the selectivity of this receptor for T-tropic and M-tropic HIV-1 strains indicates that TYMSTR might function as HIV coreceptor at both early and late stages of infection.

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ISO 690LOETSCHER, Marcel, Ali AMARA, Estelle OBERLIN, Nicole BRASS, Daniel F. LEGLER, Pius LOETSCHER, Massimo D'APUZZO, Eckart MEESE, Dominique ROUSSET, Bernhard MOSER, 1997. TYMSTR, a putative chemokine receptor selectively expressed in activated T cells, exhibits HIV-1 coreceptor function. In: Current Biology. 1997, 7(9), pp. 652-660. ISSN 0960-9822. eISSN 1879-0445. Available under: doi: 10.1016/S0960-9822(06)00292-2
BibTex
@article{Loetscher1997-09-01TYMST-37329,
  year={1997},
  doi={10.1016/S0960-9822(06)00292-2},
  title={TYMSTR, a putative chemokine receptor selectively expressed in activated T cells, exhibits HIV-1 coreceptor function},
  number={9},
  volume={7},
  issn={0960-9822},
  journal={Current Biology},
  pages={652--660},
  author={Loetscher, Marcel and Amara, Ali and Oberlin, Estelle and Brass, Nicole and Legler, Daniel F. and Loetscher, Pius and D'Apuzzo, Massimo and Meese, Eckart and Rousset, Dominique and Moser, Bernhard}
}
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    <dcterms:abstract xml:lang="eng">Background: Chemokines bind to specific receptors and mediate leukocyte migration to sites of inflammation. Recently, some chemokine receptors, notably CXCR4 and CCR5, have been shown to be essential fusion factors on target cells for infection by human immunodeficiency virus (HIV); the chemokines bound by these receptors have also been shown to act as potent inhibitors of HIV infection. Here, we describe the isolation of a novel, putative chemokine receptor.&lt;br /&gt;&lt;br /&gt;Results: We have isolated the cDNA for a putative human chemokine receptor, which we have termed TYMSTR (T-lymphocyte-expressed seven-transmembrane domain receptor). The TYMSTR gene is localized to human chromosome 3 and encodes a protein that has a high level of identity with chemokine receptors. TYMSTR mRNA was selectively expressed in interleukin-2-stimulated T lymphocytes but not in freshly isolated lymphocytes and leukocytes or related cell lines. The natural ligand for TYMSTR was not identified among 32 human chemokines and other potential ligands. Cells co-expressing TYMSTR and human CD4 fused with cells expressing envelope glycoproteins of macrophage (M)-tropic HIV-1 as well as T-cell line (T)-tropic HIV-1 isolates. Addition of infectious, T-tropic HIV-1 particles to TYMSTR/CD4-expressing cells resulted in viral entry and proviral DNA formation.&lt;br /&gt;&lt;br /&gt;Conclusions: Our findings demonstrate that TYMSTR, in combination with CD4, mediates HIV-1 fusion and entry. The high-level expression of TYMSTR in CD&lt;sup&gt;4+&lt;/sup&gt; T lymphocytes and the selectivity of this receptor for T-tropic and M-tropic HIV-1 strains indicates that TYMSTR might function as HIV coreceptor at both early and late stages of infection.</dcterms:abstract>
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