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Integrin ?4?7 Expression Increases HIV Susceptibility in Activated Cervical CD4+ T Cells by an HIV Attachment-Independent Mechanism.

ABSTRACT: BACKGROUND:CD4 T cells are crucial for the establishment and dissemination of HIV in mucosal tissues during acute infection. Studies indicate that integrin ?4?7 CD4 T cells are preferentially infected by HIV in vitro and during acute SIV infection. The integrin ?4?7 is thought to promote HIV capture by target cells; however, the role of integrin ?4?7 in HIV transmission remains controversial. In this study, we characterized immune phenotypes of human cervical T cells and examined HIV preference in integrin ?4?7 CD4 T cells. In vitro all-trans retinoic acid-differentiated peripheral CD4 T cells (atRA-differentiated cells) were included as a comparison. RESULTS:In both peripheral and cervical cells, the majority of HIV p24 cells were activated CD4 T cells expressing integrin ?4?7. Among infected atRA-differentiated cells, the frequency of CCR5 expression was higher in HIV p24 cells than in HIV p24 cells; no such difference was observed in cervical cells. Neither the cyclic hexapeptide CWLDVC nor a monoclonal antibody against integrin ?4?7 blocked HIV attachment or gp120 binding to target cells regardless of the presence of CD4, indicating that integrin ?4?7 did not facilitate HIV capture by target cells. CONCLUSIONS:Integrin ?4?7 expression increases HIV susceptibility, but the mechanism is not through promoting HIV binding to target cells.

SUBMITTER: Ding J

PROVIDER: S-EPMC4503378 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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Integrin α4β7 Expression Increases HIV Susceptibility in Activated Cervical CD4+ T Cells by an HIV Attachment-Independent Mechanism.

Ding Jian J Tasker Carley C Lespinasse Pierre P Dai Jihong J Fitzgerald-Bocarsly Patricia P Lu Wuyuan W Heller Debra D Chang Theresa Li-Yun TL

Journal of acquired immune deficiency syndromes (1999) 20150801 5

<h4>Background</h4>CD4 T cells are crucial for the establishment and dissemination of HIV in mucosal tissues during acute infection. Studies indicate that integrin α4β7 CD4 T cells are preferentially infected by HIV in vitro and during acute SIV infection. The integrin α4β7 is thought to promote HIV capture by target cells; however, the role of integrin α4β7 in HIV transmission remains controversial. In this study, we characterized immune phenotypes of human cervical T cells and examined HIV pre ...[more]

PMID: 26167616

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Project description:Blood platelets contain phospholipase D (PLD) that is rapidly activated following platelet stimulation. It is currently unclear, however, where PLD fits into the signalling cascade that leads to aggregation and secretion. Therefore we investigated the mechanism of activation of PLD in human platelets, using the formation of the PLD-specific product phosphatidylethanol as a measure of PLD activity. PLD was activated by a number of platelet agonists that also cause the activation of protein kinase C, including thrombin, collagen, the Ca2+ ionophore A23187 and the thromboxane A2-mimetic U46619. Phorbol 12-myristate 13-acetate (PMA), a direct activator of protein kinase C, also increased PLD activity. A selective inhibitor of protein kinase C, Ro-31-8220, totally blocked the stimulation of PLD by thrombin or PMA under conditions in which it also inhibited phosphorylation of pleckstrin, the major protein kinase C substrate in platelets. Ro-31-8220 additionally inhibited A23187-stimulated PLD activity, indicating that Ca2+ activation of PLD also occurs via a protein kinase C-dependent pathway. In the presence of the fibrinogen antagonist peptide RGDS, which inhibits fibrinogen binding to integrin alpha IIb beta 3 and allows little or no aggregation to occur, thrombin- and PMA-stimulated PLD activity was still observed, indicating that PLD activation is not simply a consequence of platelet aggregation. Furthermore, these agonists were able to stimulate PLD in platelets from a Glanzmann's thrombasthenia type I patient lacking the integrin alpha IIb beta 3 complex, which indicates that activation of PLD is also independent of the recruitment of integrin alpha IIb beta 3. Taken together, our results show that PLD is activated by a pathway involving protein kinase C, and suggest that PLD might be involved in signal transduction events occurring upstream of integrin alpha IIb beta 3 activation and fibrinogen binding, which are prerequisites for full platelet aggregation.

Dataset Information

Integrin ?4?7 Expression Increases HIV Susceptibility in Activated Cervical CD4+ T Cells by an HIV Attachment-Independent Mechanism.

Publications

Integrin α4β7 Expression Increases HIV Susceptibility in Activated Cervical CD4+ T Cells by an HIV Attachment-Independent Mechanism.

Similar Datasets

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