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Disguising itself -: insights into Plasmodium falciparum binding and immune evasion from the DBL crystal structure

期刊

MOLECULAR AND BIOCHEMICAL PARASITOLOGY
卷 148, 期 1, 页码 1-9

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.molbiopara.2006.03.004

关键词

malaria; antigenic variation; cytoadherence; PfEMP1; var; DBL; EBL

资金

  1. NIAID NIH HHS [T32 AI007509, R01 AI47953-01A1] Funding Source: Medline

向作者/读者索取更多资源

Duffy-binding like (DBL) domains are common to two different families of malaria proteins that are involved in parasite invasion of erythrocytes or cytoadhesion of infected erythrocytes. DBL domain crystal structures have recently been solved for two different erythrocyte binding ligands, EBA-175 and the Plasmodium knowlesi alpha Duffy binding protein. These structures reveal different mechanisms for DBL binding and erythrocyte invasion. This review summarizes recent work on DBL domain binding and immune evasion and proposes a new structural model for how these domains adapted to intense antibody surveillance at the infected erythrocyte surface. (c) 2006 Elsevier B.V. All rights reserved.

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