适应海鸥的H13禽流感病毒受体结合特异性的改变与其独特的宿主偏好相对应。

Altered receptor-binding specificity of gull-adapted H13 avian influenza viruses corresponds to their unique host preferences.

作者信息

Harada Rio, Hiono Takahiro, Igarashi Manabu, Kobayashi Daiki, Ban Hinako, Isoda Norikazu, Sakoda Yoshihiro

机构信息

Laboratory of Microbiology, Department of Disease Control, Faculty of Veterinary Medicine, Hokkaido University, Kita 18, Nishi 9, Kita-ku, Sapporo, Hokkaido, 060-0818, Japan.

Laboratory of Microbiology, Department of Disease Control, Faculty of Veterinary Medicine, Hokkaido University, Kita 18, Nishi 9, Kita-ku, Sapporo, Hokkaido, 060-0818, Japan; One Health Research Center, Hokkaido University, Kita 18, Nishi 9, Kita-ku, Sapporo, Hokkaido, 060-0818, Japan; International Collaboration Unit, International Institute for Zoonosis Control, Hokkaido University, Kita 20, Nishi 10, Kita-ku, Sapporo, Hokkaido, 001-0020, Japan; Institute for Vaccine Research and Development, Hokkaido University, Kita 21, Nishi 11, Kita-ku, Sapporo, Hokkaido, 001-0021, Japan.

出版信息

Virology. 2025 Apr;605:110460. doi: 10.1016/j.virol.2025.110460. Epub 2025 Feb 21.

DOI:10.1016/j.virol.2025.110460

PMID:39999586

Abstract

Avian influenza viruses (AIVs) recognize α2-3 sialosides as receptors. Previous studies showed that the structural diversity within α2-3 sialosides is related to the host specificity of AIVs. H13 AIVs are primarily isolated from gulls, although almost all AIV subtypes have been isolated from ducks, the natural hosts of AIVs. To elucidate the molecular basis of the host specificity of H13 viruses to gulls, the receptor-binding specificity of H13 hemagglutinins (HAs) and the distribution of viral receptors in gulls were investigated. The results revealed that recombinant HA (rHA) of H13 viruses had a binding preference for fucosylated α2-3 sialosides, which were distributed widely in the respiratory tract and intestines of gulls but not in the colon of ducks. Moreover, the receptor-binding specificity of mutant rHAs revealed that amino acids in the 130-loop and at position 227 of H13 HA were critical for the preference for fucosylated α2-3 sialosides. The results of the present study suggest that the binding specificity of H13 HA to fucosylated α2-3 sialosides is a key factor for the host susceptibility of H13 viruses to gulls.

摘要

禽流感病毒（AIVs）将α2-3唾液酸苷识别为受体。先前的研究表明，α2-3唾液酸苷内的结构多样性与AIVs的宿主特异性有关。H13 AIVs主要从海鸥中分离得到，尽管几乎所有的AIV亚型都已从AIVs的天然宿主鸭中分离得到。为了阐明H13病毒对海鸥宿主特异性的分子基础，研究了H13血凝素（HAs）的受体结合特异性以及病毒受体在海鸥中的分布。结果显示，H13病毒的重组HA（rHA）对岩藻糖基化的α2-3唾液酸苷具有结合偏好，这些唾液酸苷广泛分布于海鸥的呼吸道和肠道，但在鸭的结肠中不存在。此外，突变rHAs的受体结合特异性表明，H13 HA的130环和227位的氨基酸对于对岩藻糖基化α2-3唾液酸苷的偏好至关重要。本研究结果表明，H13 HA对岩藻糖基化α2-3唾液酸苷的结合特异性是H13病毒对海鸥宿主易感性的关键因素。