A Plasmodium falciparum S33 proline aminopeptidase is associated with changes in erythrocyte deformability
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- 作者：Fabio L. da Silvaa ; b ; 1 ; 3 ; Matthew W.A. Dixonc ; d ; 3 ; Colin M. Stacke ; 3 ; Franka Teuscherb ; Elena Taranf ; g ; Malcolm K. Jonesh ; Erica Lovash ; 2 ; Leann Tilleyc ; d ; Christopher L. Browni ; j ; Katharine R. Trenholmeb ; k ; John P. Daltona ; l ; Donald L. Gardinerb ; j ; Tina S. Skinner-Adamsi ; j ; t.skinner-adams@griffith.edu.au" class="auth_mail" title="E-mail the corresponding author
- 关键词：Prolyl aminopeptidase ; Malaria ; Plasmodium falciparum ; Erythrocyte deformability ; Cytoadherence
- 刊名：Experimental Parasitology
- 出版年：2016
- 出版时间：October 2016
- 年：2016
- 卷：169
- 期：Complete
- 页码：13-21
- 全文大小：1542 K
文摘
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The pathology of Falciparum malaria is associated with the remodeling of host RBCs.
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We investigated the role of PfPAP, a putative proline aminopeptidase in this process.
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PfPAP contains a predicted protein export element and is non-syntenic with other malaria species.
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Our data confirm that PfPAP is a proline aminopeptidase that it is exported into the host RBC.
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Genetic deletion of PfPAP suggests it plays a role in RBC rigidification and cytoadhesion