The index influenza A virus subtype H5N1 isolated from a human in 1997 differs in its receptor-binding properties from a virulent avian influenza virus.

To gain insight into the events that occur when avian influenza viruses are transmitted to humans, the receptor-binding properties of the index H5N1 influenza virus isolated from a human in 1997 and the A/turkey/Ontario/7732/66 (H5N9) virus were compared, by using a haemadsorption assay. Cells expressing the haemagglutinin (HA) of the human isolate were adsorbed by both chicken red blood cells (RBCs) and human RBCs; those expressing the avian virus HA were only adsorbed by chicken RBCs. These results indicate that human and avian influenza virus H5 HAs differ in their recognition of sialyloligosaccharides on the RBCs of different animal species. Mutational analyses indicated that differences in both the oligosaccharide chains and in the amino acid sequences around the HA receptor-binding site were responsible for this difference in receptor binding. These data further support the concept that alteration in receptor recognition is important for replication of avian viruses in humans.

[1]  Y. Guan,et al.  Antigenic differences between H5N1 human influenza viruses isolated in 1997 and 2003. , 2004, The Journal of veterinary medical science.

[2]  Y. Guan,et al.  Induction of proinflammatory cytokines in human macrophages by influenza A (H5N1) viruses: a mechanism for the unusual severity of human disease? , 2002, The Lancet.

[3]  R. Webster,et al.  Lethal H5N1 influenza viruses escape host anti-viral cytokine responses , 2002, Nature Medicine.

[4]  Ya Ha,et al.  H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes , 2002, The EMBO journal.

[5]  N. Escriou,et al.  Hemagglutinin residues of recent human A(H3N2) influenza viruses that contribute to the inability to agglutinate chicken erythrocytes. , 2001, Virology.

[6]  J. Skehel,et al.  X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[7]  Yoshihiro Kawaoka,et al.  Molecular Basis for High Virulence of Hong Kong H5N1 Influenza A Viruses , 2001, Science.

[8]  E. Nobusawa,et al.  Change in receptor-binding specificity of recent human influenza A viruses (H3N2): a single amino acid change in hemagglutinin altered its recognition of sialyloligosaccharides. , 2000, Virology.

[9]  Yoshihiro Kawaoka,et al.  Early Alterations of the Receptor-Binding Properties of H1, H2, and H3 Avian Influenza Virus Hemagglutinins after Their Introduction into Mammals , 2000, Journal of Virology.

[10]  R. Webster,et al.  The Surface Glycoproteins of H5 Influenza Viruses Isolated from Humans, Chickens, and Wild Aquatic Birds Have Distinguishable Properties , 1999, Journal of Virology.

[11]  Yoshihiro Kawaoka,et al.  Molecular Basis for the Generation in Pigs of Influenza A Viruses with Pandemic Potential , 1998, Journal of Virology.

[12]  R. Webster,et al.  Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus , 1998, The Lancet.

[13]  N. Cox,et al.  Characterization of an avian influenza A (H5N1) virus isolated from a child with a fatal respiratory illness. , 1998, Science.

[14]  Y. Kawaoka,et al.  Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks , 1997, Journal of virology.

[15]  L. Mitnaul,et al.  Receptor specificity of influenza A viruses correlates with the agglutination of erythrocytes from different animal species. , 1997, Virology.

[16]  Maricarmen García,et al.  Heterogeneity in the haemagglutinin gene and emergence of the highly pathogenic phenotype among recent H5N2 avian influenza viruses from Mexico. , 1996, The Journal of general virology.

[17]  K. Shortridge The next pandemic influenza virus? , 1995, The Lancet.

[18]  H. Klenk,et al.  Neuraminidase is essential for fowl plague virus hemagglutinin to show hemagglutinating activity. , 1995, Virology.

[19]  R. Webster,et al.  Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. , 1994, Virology.

[20]  Y. Kawaoka,et al.  Reverse genetics provides direct evidence for a correlation of hemagglutinin cleavability and virulence of an avian influenza A virus , 1994, Journal of virology.

[21]  J. Paulson,et al.  Influenza virus strains selectively recognize sialyloligosaccharides on human respiratory epithelium; the role of the host cell in selection of hemagglutinin receptor specificity. , 1993, Virus research.

[22]  Yamamura Ken-ichi,et al.  Efficient selection for high-expression transfectants with a novel eukaryotic vector , 1991 .

[23]  H. Niwa,et al.  Efficient selection for high-expression transfectants with a novel eukaryotic vector. , 1991, Gene.

[24]  G. N. Rogers,et al.  Receptor binding properties of human and animal H1 influenza virus isolates. , 1989, Virology.

[25]  S. Cusack,et al.  Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid , 1988, Nature.