Journal
VIROLOGY
Volume 386, Issue 1, Pages 61-67Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2009.01.005
Keywords
Influenza; Sialic acid; Receptors; Hemagglutinin; Tropism; Respiratory epithelium
Categories
Funding
- Washington University in St. Louis
- Eliasberg Foundation [R01 A1053629]
- Marjorie Gilbert Foundation
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Influenza A virus interacts with specific types of sialic acid during attachment and entry into susceptible cells. The precise amino acids in the hemagglutinin protein that control sialic acid binding specificity and affinity vary among antigenic subtypes. For H3 subtypes, amino acids 226 and 228 are critical for differentiating between alpha 2,3- and alpha 2,6-linked forms of sialic acid (SA). We demonstrate that position 190 of the HA from A/Udorn/307/72 (H3N2) plays an important role in the recognition of alpha 2,3-SA, as changing the residue from a glutamic acid to an aspartic acid led to alteration of red blood cell hemagglutination and a complete loss of replication in differentiated, murine trachea epithelial cell Cultures which express only alpha 2,3-SA. This amino acid change had a minimal effect on virus replication in MDCK cells, suggesting subtle changes in receptor recognition by the H3 hemagglutinin can lead to significant alterations in cell and species tropism. (c) 2009 Elsevier Inc. All rights reserved.
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