Evil versus 'eph-ective' use of ephrin-B2

被引：9

作者：

Lee, Benhur ^{[1
]}

Ataman, Zeynep Akyol ^{[1
]}

Jin, Lei ^{[1
]}

机构：

[1] Univ Calif Los Angeles, David Geffen Sch Med, Dept Microbiol Mol Genet & Immunol, Los Angeles, CA 90095 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2008年 / 15卷 / 06期

关键词：

D O I：

10.1038/nsmb0608-540

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：

Crystal structures of the Nipah and Hendra virus attachment protein complexed with ephrin-B2 shed light on the apparent paradox of ephrin-B2's flexibility for binding multiple receptors. Surprisingly, the switch from the use of glycan-based to protein-based receptors seems to have evolved independently from other protein-receptor–using paramyxoviruses such as the measles virus.

引用

收藏

页码：540 / 542

页数：4

相关论文

共 18 条

[1] Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus [J].

Bonaparte, MI ;

Dimitrov, AS ;

Bossart, KN ;

Crameri, G ;

Mungal, BA ;

Bishop, KA ;

Choudhry, V ;

Dimitrov, DS ;

Wang, LF ;

Eaton, BT ;

Broder, CC .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (30) :10652-10657

[2] Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2 [J].

Bowden, Thomas A. ;

Aricescu, A. Radu ;

Gilbert, Robert J. C. ;

Grimes, Jonathan M. ;

Jones, E. Yvonne ;

Stuart, David I. .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2008, 15 (06) :567-572

[3] Structural and biophysical characterization of the EphB4•ephrinB2 protein-protein interaction and receptor specificity [J].

Chrencik, Jill E. ;

Brooun, Alexei ;

Kraus, Michelle L. ;

Recht, Michael I. ;

Kolatkar, Anand R. ;

Han, Gye Won ;

Seifert, Jan Marcus ;

Widmer, Hans ;

Auer, Manfred ;

Kuhn, Peter .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (38) :28185-28192

[4] Structure of the measles virus hemagglutinin [J].

Colf, Leremy A. ;

Juo, Z. Sean ;

Garcia, K. Christopher .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2007, 14 (12) :1227-1228

[5] Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein [J].

Corey, Elizabeth A. ;

Iorio, Ronald M. .

JOURNAL OF VIROLOGY, 2007, 81 (18) :9900-9910

[6] Evidence of a potential receptor-binding site on the Nipah virus G protein (NiV-G): Identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural model [J].

Guillaume, Vanessa ;

Aslan, Harnide ;

Ainouze, Michelle ;

Guerbois, Mathilde ;

Wild, T. Fabian ;

Buckland, Robin ;

Langedijk, Johannes P. M. .

JOURNAL OF VIROLOGY, 2006, 80 (15) :7546-7554

[7] Crystal structure of measles virus hemagglutinin provides insight into effective vaccines [J].

Hashiguchi, Takao ;

Kajikawa, Mizuho ;

Maita, Nobuo ;

Takeda, Makoto ;

Kuroki, Kimiko ;

Sasaki, Kaori ;

Kohda, Daisuke ;

Yanagi, Yusuke ;

Maenaka, Katsumi .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (49) :19535-19540

[8] Crystal structure of an Eph receptor-ephrin complex [J].

Himanen, JP ;

Rajashankar, KR ;

Lackmann, M ;

Cowan, CA ;

Henkemeyer, M ;

Nikolov, DB .

NATURE, 2001, 414 (6866) :933-938

[9] Paramyxovirus membrane fusion: Lessons from the F and HN atomic structures [J].

Lamb, RA ;

Paterson, RG ;

Jardetzky, TS .

VIROLOGY, 2006, 344 (01) :30-37

[10] Addition of N-glycans in the stalk of the newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion [J].

Melanson, VR ;

Iorio, RM .

JOURNAL OF VIROLOGY, 2006, 80 (02) :623-633