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• W2085536315 startingPage "26666" @default.
• W2085536315 abstract "Pigs can act as intermediate hosts by which reassorted influenza A virus (IAV) strains can be transmitted to humans and cause pandemic influenza outbreaks. The innate host defense component surfactant protein D (SP-D) interacts with glycans on the hemagglutinin of IAV and contributes to protection against IAV infection in mammals. This study shows that a recombinant trimeric neck lectin fragment derived from porcine SP-D (pSP-D) exhibits profound inhibitory activity against IAV, in contrast to comparable fragments derived from human SP-D. Crystallographic analysis of the pSP-D fragment complexed with a viral sugar component shows that a unique tripeptide loop alters the lectin site conformation of pSP-D. Molecular dynamics simulations highlight the role of this flexible loop, which adopts a more stable conformation upon sugar binding and may facilitate binding to viral glycans through contact with distal portions of the branched mannoside. The combined data demonstrate that porcine-specific structural features of SP-D contribute significantly to its distinct anti-IAV activity. These findings could help explain why pigs serve as important reservoirs for newly emerging pathogenic IAV strains." @default.
• W2085536315 created "2016-06-24" @default.
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• W2085536315 date "2012-08-01" @default.
• W2085536315 modified "2023-10-06" @default.
• W2085536315 title "A Unique Sugar-binding Site Mediates the Distinct Anti-influenza Activity of Pig Surfactant Protein D" @default.
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• W2085536315 doi "https://doi.org/10.1074/jbc.m112.368571" @default.
• W2085536315 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3411006" @default.
• W2085536315 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22685299" @default.
• W2085536315 hasPublicationYear "2012" @default.
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