Mutations flanking the carbohydrate binding site of surfacta…

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  • DOI 10.1152/ajplung.00035.2014
  • PMID https://pubmed.ncbi.nlm.nih.gov/24705721
  • OpenAlex ID W2332762308
  • Type Article
  • Language EN
  • Published 05 Apr 2014
  • Volume 306 (11)
  • Pages L1036–L1044
  • Source American Journal of Physiology-Lung Cell…
  • Publisher American Physical Society
  • FWCI 1.01
  • Countries 1
  • Institutions 4
  • Added 24 Jun 2016
  • Updated 27 Oct 2026
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Mutations flanking the carbohydrate binding site of surfactant protein D confer antiviral activity for pandemic influenza A viruses

Article 2014 EN Green

We recently reported that a trimeric neck and carbohydrate recognition domain (NCRD) fragment of human surfactant protein D (SP-D), a host defense lectin, with combinatorial substitutions at the 325 and 343 positions (D325A+R343V) exhibits markedly increased antiviral activity for seasonal strains of influenza A virus (IAV). The NCRD binds to glycan-rich viral envelope proteins including hemagglut…

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1.01

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Authors & Affiliations
11 authors
#AuthorInstitutionsORCID
1 Nikolaos M. Nikolaidis University of Cincinnati (US)
2 Mitchell R. White Boston University (US)
3 Kimberly Allen Washington University in St. L… (US) —
4 Shweta Tripathi Boston University (US)
5 Li Qi National Institute of Allergy … (US)
6 Barbara McDonald Washington University in St. L… (US) —
7 Jeffery K. Taubenberger National Institute of Allergy … (US)
8 Barbara A. Seaton Boston University (US)
9 Francis X. McCormack University of Cincinnati (US)
10 Erika C. Crouch Washington University in St. L… (US) —
11 Kevan L. Hartshorn Corresponding Boston University (US)

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