Journal
VIROLOGY
Volume 378, Issue 2, Pages 282-291Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2008.05.023
Keywords
paramyxovirus; parainfluenza virus 5; hemagglutinin-neuramidase (HN); virus entry; sialic acid; membrane fusion/HN stalk
Categories
Funding
- NIH [GM-61050, AI-23173, R01 RR022200-01A1]
- Robert J. Kleberg Jr. and Helen C. Kleberg Foundation
- NSF [TGMCB070038]
- NCI [P30 CA054174]
- UTHSCSA ERC
- NATIONAL CANCER INSTITUTE [P30CA054174] Funding Source: NIH RePORTER
- NATIONAL CENTER FOR RESEARCH RESOURCES [R01RR022200] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI023173] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM061050] Funding Source: NIH RePORTER
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The mechanism by which the paramyxovirus hemagglutinin-neuraminidase (HN) protein couples receptor binding to activation of virus entry remains to be fully understood, but the FIN stalk is thought to play an important role in the process. We have characterized ectodomain constructs of the parainfluenza virus 5 HN to understand better the underlying architecture and oligomerization properties that may influence HN functions. The PIV 5 neuraminidase (NA) domain is monomeric whereas the ectodomain forms a well-defined tetramer. The HN stalk also forms tetramers and higher order oligomers with high alpha-helical content. Together, the data indicate that the globular NA domains form weak intersubunit interactions at the end of the HN stalk tetramer, while stabilizing the stalk and overall oligomeric state of the ectodomain. Electron microscopy of the HN ectodomain reveals flexible arrangements of the NA and stalk domains, which may be important for understanding how these two HN domains impact virus entry. (C) 2008 Elsevier Inc. All rights reserved.
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