6-sulfo sialyl Lewis X is the common receptor determinant recognized by H5, H6, H7 and H9 influenza viruses of terrestrial poultry

Abstract

Background: Influenza A viruses of domestic birds originate from the natural reservoir in aquatic birds as a result of interspecies transmission and adaptation to new host species. We previously noticed that influenza viruses isolated from distinct orders of aquatic and terrestrial birds may differ in their fine receptor-binding specificity by recognizing the structure of the inner parts of Neu5Acα2-3Gal-terminated sialyloligosaccharide receptors. To further characterize these differences, we studied receptor-binding properties of a large panel of influenza A viruses from wild aquatic birds, poultry, pigs and horses.

Recent evolution of equine influenza and the origin of canine influenza

“…The strong preference observed for α2,3-linked over α2,6-linked sialosides is in agreement with previously reported results for equine viruses (17). Similarly, the greater avidities of equine viruses for analogs containing sulfated GlcNAc3 residues have been reported before (18)(19)(20). Ef virus binds 3′ sialylactosamine (3′SLN) with about 1/3rd the avidity of Ee and the other three analogs, Sialyl Lewis X (SLe x ), sulfated Sialyl Lewis X (Su-SLe x ), and Su-3′SLN, with about 1/10th the avidity of Ee (Fig.…”

“…S4). This is probably a result of the Trp-222→Leu substitution in C vs. Ef/Ee, a probability that would be consistent with the observed importance of the size of the 222 side chain in influencing receptor binding affinity of avian HAs (19,20). Conversely, in complexes formed by C and Ee HAs with Su-SLe X , the length of this hydrogen bond appeared very similar (2.7 Å and 2.6 Å, respectively), possibly because of the interaction of Lys-193 with the SO4 group (Fig.…”

Immunization with live nonpathogenic H5N3 duck influenza virus protects chickens against highly pathogenic H5N1 virus

“…Inefficient replication of aquatic birds viruses in chickens depends, at least partially, on the differences in receptors on target cells in these species . Adaptation of duck viruses to gallinaceous poultry is accompanied by changes in the viral receptor specificity and neuraminidase activity, owing to acquisition by poultryadapted viruses of additional glycosylation sites near the receptor-binding site of the HA and to deletions in the stem region of their NA (Matrosovich et al, 1999(Matrosovich et al, , 2001Banks et al, 2001;Gambaryan et al, 2008). These adaptive changes in the HA and NA of poultry-adapted viruses occur before the acquisition of multibasic cleavage site and high pathogenicity, which is the final stage in the evolution of AIV in gallinaceous poultry.…”

A Single Amino Acid Substitution in the Hemagglutinin of H3N2 Subtype Influenza A Viruses Is Associated with Resistance to the Long Pentraxin PTX3 and Enhanced Virulence in Mice

“…Moreover, H5N1 viruses display clear HA preference for SIAa (2,3) (34, 35) yet were resistant to PTX3, even in the presence of NAI. Some avian viruses discriminate between the core structures of oligosaccharides (50), and HA-glycan conformation analysis suggests that the size and shape of SIA-bearing glycans, rather than specific linkage, are important for H5-mediated recognition (51). Therefore, it may be that the type of SIA presented by PTX3 is not recognized by the H5 HA, suggesting further complexity in the interplay between the fine specificity of the viral HA and the particular SIAa(2,3)-rich glycans expressed by PTX3.…”