Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses

被引：115

作者：

Abraham, Jonathan ^{[1
,2
]}

Corbett, Kevin D. ^{[3
]}

Farzan, Michael ^{[4
]}

Choe, Hyeryun ^{[2
]}

Harrison, Stephen C. ^{[1
,3
,5
]}

机构：

[1] Harvard Univ, Sch Med, Mol Med Lab, Boston, MA 02115 USA

[2] Harvard Univ, Childrens Hosp, Sch Med, Dept Med, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

[4] Harvard Univ, Sch Med, New England Primate Ctr, Dept Microbiol & Mol Genet, Southborough, MA 01772 USA

[5] Harvard Univ, Sch Med, Howard Hughes Med Inst, Boston, MA 02115 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2010年 / 17卷 / 04期

基金：

美国国家卫生研究院;

关键词：

STABLE SIGNAL PEPTIDE; MULTIPLE SEQUENCE ALIGNMENT; CRYSTAL-STRUCTURE; ENVELOPE GLYCOPROTEIN; LOW PH; VIRUS; PHYLOGENY; ENTRY; EVOLUTION; SUBUNIT;

D O I：

10.1038/nsmb.1772

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

New World hemorrhagic fever arenaviruses are rodent-borne agents that cause severe human disease. The GP1 subunit of the surface glycoprotein mediates cell attachment through transferrin receptor 1 (TfR1). We report the structure of Machupo virus (MACV) GP1 bound with human TfR1. Atomic details of the GP1-TfR1 interface clarify the importance of TfR1 residues implicated in New World arenavirus host specificity. Analysis of sequence variation among New World arenavirus GP1s and their host-species receptors, in light of the molecular structure, indicates determinants of viral zoonotic transmission. Infectivities of pseudoviruses in cells expressing mutated TfR1 confirm that contacts at the tip of the TfR1 apical domain determine the capacity of human TfR1 to mediate infection by particular New World arenaviruses. We propose that New World arenaviruses that are pathogenic to humans fortuitously acquired affinity for human TfR1 during adaptation to TfR1 of their natural hosts.

引用

页码：438 / U76

页数：8

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