Focus
Focus on Measles Virus
The NSMB Web Focus on Measles Virus highlights current developments in our understanding of the interaction between the viral attachment protein MVH and its host cell receptor SLAM, and the conformational changes in MVH that trigger fusion of viral and cellular membranes. The Web Focus features a News and Views piece that puts these findings in context, as well as previous studies on MVH and on the attachment protein from other paramyxoviruses, published in our pages. This body of work is of interest to structural and molecular biologists, as well as virologists and clinical researchers.
News and Views
Measles virus fusion machinery shifts into gear-
Michael B.A. Oldstone & Erica Ollmann Saphire
Two recent papers present contrasting models for the machinations of the measles virus attachment protein. Here we discuss how these reports illuminate possible intersubunit motions made by the protein as it drives the fusion of viral and cellular membranes during infection, furthering our understanding of this global scourge.
Nature Structural & Molecular Biology 18, 115-116 (2011)
doi:10.1038/nsmb0211-115
Research Articles
The heads of the measles virus attachment protein move to transmit the fusion-triggering signal-
Chanakha K Navaratnarajah, Numan Oezguen, Levi Rupp, Leah Kay, Vincent HJ Leonard, Werner Braun & Roberto Cattaneo
Binding of measles virus hemagglutinin (MVH) to its cellular receptors triggers the activation of the fusion protein. The conformational changes of MVH upon receptor binding are examined by locking the dimers using disulfide bonds, or by pulling on appropriately positioned hexahistidine tags. The results indicate that the dimer interface is pulled apart after receptor binding by twisting of the MVH heads.
Nature Structural & Molecular Biology 18, 128-134 (2011)
doi:10.1038/nsmb.1967
Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM-
Takao Hashiguchi, Toyoyuki Ose, Marie Kubota, Nobuo Maita, Jun Kamishikiryo, Katsumi Maenaka & Yusuke Yanagi
The measles virus hemagglutinin (MVH) promotes viral attachment to host cells via interaction with signaling lymphocyte activation molecule (SLAM). The crystal structure of MVH head domain in complex with the distal domain of SLAM, together with functional work, reveals the details of this interaction and explains the effectiveness of the currently used vaccine.
Nature Structural & Molecular Biology 18, 135-141 (2011)
doi:10.1038/nsmb.1969
Structure of the measles virus hemagglutinin bound to the CD46 receptor-
César Santiago, María L Celma, Thilo Stehle & José M Casasnovas
Nature Structural & Molecular Biology 18, 124-129 (2011)
doi:10.1038/nsmb.1726
Cellular infection with measles virus starts with the binding of the viral hemagglutinin (MVH) to host cell receptors (CD46 or SLAM, depending on the measles strain). The crystal structure of MVH bound to the membrane distal extracellular domains of CD46 (SCR1 and SCR2) is now described, shedding light on this important interaction.
Structure of the measles virus hemagglutinin-
Leremy A Colf, Z Sean Juo & K Christopher Garcia
Nature Structural & Molecular Biology 14, 1227-1228 (2007)
doi:10.1038/nsmb1342
Measles virus is highly contagious, infecting 20 million people per year. The structure of measles virus hemagglutinin, the glycoprotein responsible for binding to host cell surface receptors, may help in the development of drug therapies.
Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2-
Thomas A Bowden, A Radu Aricescu, Robert J C Gilbert, Jonathan M Grimes, E Yvonne Jones & David I Stuart
Nature Structural & Molecular Biology 15, 567-572 (2008)
doi:10.1038/nsmb.1435
Henipaviruses can cause disease with high mortality rates in humans and other mammals. The crystal structures of the attachment glycoprotein from 2 virus types in this genus, Nipah and Hendra, in complex with the ectodomain of human receptor ephrin-B2 now reveal an extensive protein-protein interface that contrasts with other paramyxoviruses, and has implications for antiviral drug design.
News and Views
Evil versus 'eph-ective' use of ephrin-B2 -
Benhur Lee, Zeynep Akyol Ataman & Lei Jin
Nature Structural & Molecular Biology 15, 540-542 (2008)
doi:10.1038/nsmb0608-540
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.
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