ZBiotechMicrobiologyDefining the substrates of H3N8 AVI mutants
Microbiology

Defining the substrates of H3N8 AVI mutants

Z Biotech’s Neu5Gc & Neu5Ac N-glycan microarray helps scientists delineate the varying glycan receptor binding specificities of diverse H3N8 avian influenza virus mutants.

Highlights

Array:Neu5Ac & Neu5Gc
Field:Microbiology
Study:protein-glycan interaction

H3N8 avian influenza viruses (AIVs) are known to be present in wild bird species, yet their potential for transmission amongst mammals has not been adequately explored. Capitalizing on a collection of H3N8 AIVs sourced from wild bird reservoirs, Zhang and colleagues successfully sequenced the genomes of these viruses, subsequently classifying eight H3N8 variants into seven distinct genotypes based on genomic diversity. Their investigation revealed that a notable majority – six out of the eight viruses had developed the capacity to bind to human-type receptors. However, the affinity of these viruses for α-2,6-linked sialic acids (SAs) was lesser than that for α-2,3-linked SAs, indicating a shift in the SA binding preference of these viruses. In subsequent animal transmission experiments, the team discovered that three of the viruses could efficiently infect direct-contact guinea pigs without any prior adaptation. Additionally, one virus exhibited proficient transmission via respiratory droplets in guinea pigs, but this was not observed in ferrets. In a significant finding, the researchers identified a PB1 S524G mutation that endowed the T222 virus with airborne transmissibility between ferrets. This same mutation was found to slightly heighten viral pathogenicity in mice when compared to the wild type. Through these investigations, the researchers have illuminated the molecular and transmissibility landscape of H3N8 AIVs. Their work underscores the necessity of maintaining vigilant surveillance of H3N8 AIVs circulating in bird populations.

Z Biotech’s Neu5Gc & Neu5Ac N-glycan microarray has provided scientists with the tools to uncover a binding shift from α-2,6-linked to α-2,3-linked SAs in H3N8 AVIs. It facilitated researchers in accurately identifying the specificity of AVI receptor interactions with glycans. By employing the Neu5Ac and Neu5Gc N-glycan microarray, scientists can swiftly and precisely determine the exact glycans to which the viral receptor binds, along with the specificity of the interaction. Hence, the Neu5Ac and Neu5Gc N-glycan microarray proves to be an essential tool in unveiling critical aspects of viral behavior.

Reference

Zhang, X. et al. PB1 S524G mutation of wild bird-origin H3N8 influenza A virus enhances virulence and fitness for transmission in mammals. Emerg. Microbes Infect. 10, 1038–1051 (2021).