Department of Laboratory Medicine, University of Gothenburg, Sahlgrenska University Hospital, Vita Stråket 12, Gothenburg SE-413 45, Sweden.
Laboratory of Clinical Chemistry, Sahlgrenska University Hospital, Bruna Stråket 16, Gothenburg SE-413 45, Sweden.
Glycobiology. 2024 Apr 1;34(3). doi: 10.1093/glycob/cwad098.
Influenza A virus (IAV) pandemics result from interspecies transmission events within the avian reservoir and further into mammals including humans. Receptor incompatibility due to differently expressed glycan structures between species has been suggested to limit zoonotic IAV transmission from the wild bird reservoir as well as between different bird species. Using glycoproteomics, we have studied the repertoires of expressed glycan structures with focus on putative sialic acid-containing glycan receptors for IAV in mallard, chicken and tufted duck; three bird species with different roles in the zoonotic ecology of IAV. The methodology used pinpoints specific glycan structures to specific glycosylation sites of identified glycoproteins and was also used to successfully discriminate α2-3- from α2-6-linked terminal sialic acids by careful analysis of oxonium ions released from glycopeptides in tandem MS/MS (MS2), and MS/MS/MS (MS3). Our analysis clearly demonstrated that all three bird species can produce complex N-glycans including α2-3-linked sialyl Lewis structures, as well as both N- and O- glycans terminated with both α2-3- and α2-6-linked Neu5Ac. We also found the recently identified putative IAV receptor structures, Man-6P N-glycopeptides, in all tissues of the three bird species. Furthermore, we found many similarities in the repertoires of expressed receptors both between the bird species investigated and to previously published data from pigs and humans. Our findings of sialylated glycan structures, previously anticipated to be mammalian specific, in all three bird species may have major implications for our understanding of the role of receptor incompatibility in interspecies transmission of IAV.
甲型流感病毒(IAV)大流行是由禽类宿主中的种间传播事件以及进一步传播到哺乳动物(包括人类)引起的。由于物种间糖蛋白结构表达的糖链结构不同,导致流感病毒从野生鸟类宿主以及不同鸟类物种之间的种间传播受到限制。本研究使用糖蛋白质组学研究了表达的糖链结构谱,重点研究了鸭、鸡和绒鸭三种在 IAV 人畜共患病生态中具有不同作用的鸟类的潜在含唾液酸的糖蛋白受体。所使用的方法将特定的糖链结构精确地定位到鉴定的糖蛋白的糖基化位点,并且还通过仔细分析串联 MS/MS(MS2)和 MS/MS/MS(MS3)中从糖肽释放的氧鎓离子,成功地区分了α2-3-和α2-6 连接的末端唾液酸。我们的分析清楚地表明,所有三种鸟类都可以产生复杂的 N-糖链,包括α2-3 连接的唾液酸化 Lewis 结构,以及同时用α2-3-和α2-6 连接的 Neu5Ac 末端的 N-和 O-糖链。我们还在三种鸟类的所有组织中发现了最近鉴定的潜在 IAV 受体结构,即 Man-6P N-糖肽。此外,我们发现所研究的鸟类物种之间以及以前发表的猪和人类数据之间表达的受体谱存在许多相似之处。我们在所有三种鸟类中发现了以前预期为哺乳动物特有的唾液酸化糖链结构,这可能对我们理解受体不兼容性在 IAV 种间传播中的作用具有重要意义。