scholarly journals Use of AAScatterPlot tool for monitoring the evolution of the hemagglutinin cleavage site in H9 avian influenza viruses

2017 ◽  
Vol 33 (16) ◽  
pp. 2431-2435 ◽  
Author(s):  
Donald W Lee ◽  
Gary R Whittaker
Keyword(s):  
Avian Influenza ◽  
Cleavage Site ◽  
Influenza Viruses ◽  
Avian Influenza Viruses

scholarly journals Alterations in Hemagglutinin Receptor-Binding Specificity Accompany the Emergence of Highly Pathogenic Avian Influenza Viruses

2015 ◽  
Vol 89 (10) ◽  
pp. 5395-5405 ◽  
Author(s):  
Alla Heider ◽  
Larisa Mochalova ◽  
Timm Harder ◽  
Alexander Tuzikov ◽  
Nicolai Bovin ◽  
...  
Keyword(s):  
Avian Influenza ◽  
Receptor Binding ◽  
Cleavage Site ◽  
Highly Pathogenic Avian Influenza ◽  
Binding Specificity ◽  
Influenza Viruses ◽  
Avian Influenza Viruses ◽  
Highly Pathogenic ◽  
Pathogenic Avian Influenza ◽  
Receptor Binding Specificity

ABSTRACTHighly pathogenic avian influenza viruses (HPAIVs) of hemagglutinin H5 and H7 subtypes emerge after introduction of low-pathogenic avian influenza viruses (LPAIVs) from wild birds into poultry flocks, followed by subsequent circulation and evolution. The acquisition of multiple basic amino acids at the endoproteolytical cleavage site of the hemagglutinin (HA) is a molecular indicator for high pathogenicity, at least for infections of gallinaceous poultry. Apart from the well-studied significance of the multibasic HA cleavage site, there is only limited knowledge on other alterations in the HA and neuraminidase (NA) molecules associated with changes in tropism during the emergence of HPAIVs from LPAIVs. We hypothesized that changes in tropism may require alterations of the sialyloligosaccharide specificities of HA and NA. To test this hypothesis, we compared a number of LPAIVs and HPAIVs for their HA-mediated binding and NA-mediated desialylation of a set of synthetic receptor analogs, namely, α2-3-sialylated oligosaccharides. NA substrate specificity correlated with structural groups of NAs and did not correlate with pathogenic potential of the virus. In contrast, all HPAIVs differed from LPAIVs by a higher HA receptor-binding affinity toward the trisaccharides Neu5Acα2-3Galβ1-4GlcNAcβ (3′SLN) and Neu5Acα2-3Galβ1-3GlcNAcβ (SiaLec) and by the ability to discriminate between the nonfucosylated and fucosylated sialyloligosaccharides 3′SLN and Neu5Acα2-3Galβ1-4(Fucα1-3)GlcNAcβ (SiaLex), respectively. These results suggest that alteration of the receptor-binding specificity accompanies emergence of the HPAIVs from their low-pathogenic precursors.IMPORTANCEHere, we have found for the first time correlations of receptor-binding properties of the HA with a highly pathogenic phenotype of poultry viruses. Our study suggests that enhanced receptor-binding affinity of HPAIVs for a typical “poultry-like” receptor, 3′SLN, is provided by substitutions in the receptor-binding site of HA which appeared in HA of LPAIVs in the course of transmission of LPAIVs from wild waterfowl into poultry flocks, with subsequent adaptation in poultry. The identification of LPAIVs with receptor characteristics of HPAIVs argues that the sialic acid-binding specificity of the HA may be used as a novel phenotypic marker of HPAIVs.

scholarly journals Molecular Determinants within the Surface Proteins Involved in the Pathogenicity of H5N1 Influenza Viruses in Chickens

2004 ◽  
Vol 78 (18) ◽  
pp. 9954-9964 ◽  
Author(s):  
Diane J. Hulse ◽  
Robert G. Webster ◽  
Rupert J. Russell ◽  
Daniel R. Perez
Keyword(s):  
Amino Acids ◽  
Avian Influenza ◽  
Cleavage Site ◽  
Glycosylation Site ◽  
Influenza Viruses ◽  
Surface Proteins ◽  
Avian Influenza Viruses ◽  
Highly Pathogenic ◽  
H5n1 Influenza ◽  
High Pathogenicity

ABSTRACT Although it is established that the cleavage site and glycosylation patterns in the hemagglutinin (HA) play important roles in determining the pathogenicity of H5 avian influenza viruses, some viruses exist that are not highly pathogenic despite possessing the known characteristics of high pathogenicity (i.e., their HA contains multiple basic amino acids at the cleavage site and has glycosylation patterns similar to that of the highly pathogenic H5 viruses). Currently little is known about the H5N1 viruses that fall into this intermediate category of pathogenicity. We have identified strains of H5N1 avian influenza viruses that have markers typical of high pathogenicity but distinctly differ in their ability to cause disease and death in chickens. By analyzing viruses constructed by reverse-genetic methods and containing recombinant HAs, we established that amino acids 97, 108, 126, 138, 212, and 217 of HA, in addition to those within the cleavage site, affect pathogenicity. Further investigation revealed that an additional glycosylation site within the neuraminidase (NA) protein globular head contributed to the high virulence of the H5N1 virus. Our findings are in agreement with previous observations that suggest that the activities of the HA and NA proteins are functionally linked.

scholarly journals H9 avian influenza reassortant with engineered polybasic cleavage site displays a highly pathogenic phenotype in chicken

2011 ◽  
Vol 92 (8) ◽  
pp. 1843-1853 ◽  
Author(s):  
Sandra Gohrbandt ◽  
Jutta Veits ◽  
Angele Breithaupt ◽  
Jana Hundt ◽  
Jens P. Teifke ◽  
...  
Keyword(s):  
Avian Influenza ◽  
Cleavage Site ◽  
Influenza Viruses ◽  
The Other ◽  
Virulence Determinants ◽  
Avian Influenza Viruses ◽  
Highly Pathogenic ◽  
Pathogenic Avian Influenza ◽  
Ha Gene ◽  
Virulence Potential

In the field, highly pathogenic avian influenza viruses (HPAIV) originate from low-pathogenic strains of the haemagglutinin (HA) serotypes H5 and H7 that have acquired a polybasic HA cleavage site. This observation suggests the presence of a cryptic virulence potential of H5 and H7 low-pathogenic avian influenza viruses (LPAIV). Among all other LPAIV, the H9N2 strains are of particular relevance as they have become widespread across many countries in several avian species and have been transmitted to humans. To assess the potential of these strains to transform into an HPAIV, we introduced a polybasic cleavage site into the HA of a contemporary H9N2 isolate. Whereas the engineered polybasic HA cleavage site mutant remained a low-pathogenic strain like its parent virus, a reassortant expressing the modified H9 HA with engineered polybasic cleavage site and all the other genes from an H5N1 HPAIV became highly pathogenic in chicken with an intravenous pathogenicity index of 1.23. These results suggest that an HPAIV with a subtype other than H5 or H7 would only emerge under conditions where the HA gene could acquire a polybasic cleavage site and the other viral genes carry additional virulence determinants.

scholarly journals SequenceAnalysis of Recent H7 Avian Influenza Viruses Associated with ThreeDifferent Outbreaks in Commercial Poultry in the UnitedStates

2003 ◽  
Vol 77 (24) ◽  
pp. 13399-13402 ◽  
Author(s):  
Erica Spackman ◽  
Dennis A. Senne ◽  
Sherrill Davison ◽  
David L. Suarez
Keyword(s):  
Amino Acids ◽  
Avian Influenza ◽  
Cleavage Site ◽  
Influenza Viruses ◽  
Avian Influenza Viruses ◽  
Receptor Binding Site ◽  
Highly Pathogenic ◽  
Genetic Features ◽  
Commercial Poultry ◽  
Live Bird

ABSTRACT The hemagglutinin (HA) and neuraminidase (NA) genes of H7 avian influenza virus (AIV) isolated between 1994 and 2002 from live-bird markets (LBMs) in the northeastern United States and from three outbreaks in commercial poultry have been characterized. Phylogenetic analysis of the HA and NA genes demonstrates that the isolates from commercial poultry were closely related to the viruses circulating in the LBMs. Also, since 1994, two distinguishing genetic features have appeared in this AIV lineage: a deletion of 17 amino acids in the NA protein stalk region and a deletion of 8 amino acids in the HA1 protein which is putatively in part of the receptor binding site. Furthermore, analysis of the HA cleavage site amino acid sequence, a marker for pathogenicity in chickens and turkeys, shows a progression toward a cleavage site sequence that fulfills the molecular criteria for highly pathogenic AIV.

Virulence-associated sequence duplication at the hemagglutinin cleavage site of avian influenza viruses

1997 ◽  
Vol 49 (2) ◽  
pp. 173-186 ◽  
Author(s):  
Michael L. Perdue ◽  
Maricarmen Garcı́a ◽  
Dennis Senne ◽  
M. Fraire
Keyword(s):  
Avian Influenza ◽  
Cleavage Site ◽  
Influenza Viruses ◽  
Avian Influenza Viruses

scholarly journals Amino acids adjacent to the haemagglutinin cleavage site are relevant for virulence of avian influenza viruses of subtype H5

2010 ◽  
Vol 92 (1) ◽  
pp. 51-59 ◽  
Author(s):  
S. Gohrbandt ◽  
J. Veits ◽  
J. Hundt ◽  
J. Bogs ◽  
A. Breithaupt ◽  
...  
Keyword(s):  
Amino Acids ◽  
Avian Influenza ◽  
Cleavage Site ◽  
Influenza Viruses ◽  
Avian Influenza Viruses

Avian influenza viruses in wild birds at the Jeziorsko reservoir in Poland in 2008-2010

2012 ◽  
Vol 15 (2) ◽  
pp. 323-328 ◽  
Author(s):  
K. Śmietanka ◽  
Z. Minta ◽  
R. Włodarczyk ◽  
K. Wyrostek ◽  
M. Jóźwiak ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Amino Acid ◽  
Avian Influenza ◽  
Avian Influenza Virus ◽  
Cleavage Site ◽  
Wild Birds ◽  
Influenza Viruses ◽  
Surveillance Study ◽  
Avian Influenza Viruses ◽  
Amino Acid Motif

Avian influenza viruses in wild birds at the Jeziorsko reservoir in Poland in 2008-2010 During a 3-year surveillance study for avian influenza virus (AIV) infections at the Jeziorsko reservoir in central Poland, 549 oropharyngeal or cloacal swabs from 366 birds of 14 species belonging to 3 orders (Anseriformes, Charadriiformes and Gruiformes) were tested. AIV was detected in 14 birds (3.8%): Common Teals (12x), Mallard (1x) and Garganey (1x). Three potentially dangerous H5 AIV were detected in Common Teals (2x) and Garganey (1x) but all of them revealed a low pathogenic pathotype. A unique cleavage site amino acid motif PQREIR*GLF was found in one H5 isolate from a Garganey.

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