Mutations flanking the carbohydrate binding site of surfactant protein D confer antiviral activity for pandemic influenza A viruses.
PMID: 24705721
2014
American journal of physiology. Lung cellular and molecular physiology
Abstract: D325A+R343V and D325S+R343V also strongly inhibited HA activity, and markedly aggregated, the 1968 pandemic H3N2 strain, Aichi68.
Abstract: D325S+R343V significantly reduced viral loads and mortality of mice infected with Aichi68, whereas wild-type SP-D NCRD did not.
Abstract: Importantly, we now show that D325A+R343V and D325S+R343V inhibited Cal09 H1N1 and related strains, and reduced uptake of Cal09 by epithelial cells.
Abstract: The activity of the double mutants was significantly greater than that of either single mutant (D325A/S or
Molecular mechanisms of inhibition of influenza by surfactant protein D revealed by large-scale molecular dynamics simulation.
Abstract: Furthermore, the blocking mechanism of HA differs for WT and D325A+R343V because of alternate glycan binding modes.
Abstract: On the basis of the D325A+R343V-Man9 structure and other crystallographic data, models of complexes between HA and WT or D325A+R343V were produced and subjected to molecular dynamics.
Abstract: Simulations reveal that whereas WT and D325A+R343V both block the sialic acid receptor site of HA, the D325A+R343V complex is more stable, with stronger binding caused by additional hydrogen bonds and hy
Viral aggregating and opsonizing activity in collectin trimers.
PMID: 19837850
2010
American journal of physiology. Lung cellular and molecular physiology
Abstract: The most effective substitution involved replacement of arginine 343 with valine (hSP-D-NCRD/R343V).
Abstract: These effects were further increased by cross-linking of hSP-D-NCRD/R343V trimers with MAbs directed against areas of the hSP-D-NCRD not involved in viral binding.
Abstract: Unlike the wild-type human SP-D hSP-D-NCRD, hSP-D-NCRD/R343V also induced viral aggregation.
Abstract: hSP-D-NCRD/R343V greatly increased viral uptake by neutrophils and monocytes and also potentiated neutrophil respiratory burst responses.
Increasing antiviral activity of surfactant protein d trimers by introducing residues from bovine serum collectins: dissociation of mannan-binding and antiviral activity.
PMID: 20591072
2010
Scandinavian journal of immunology
Abstract: We now show, however, that combined mutants containing the RAK insertion and R343V or R343I substitutions have greatly increased mannan-binding ability, but lower IAV binding or inhibiting activity than mutants containing R343V or R343I substitutions only.
Method: Using the wild type hSP-D-NCRD and R343V mutant we not found evidence of aggregation on storage of the proteins.
Result: All of the serum collectins have a hydrophobic residue at position 343 (SP-D numbering), and we have previously shown that hSP-D-NCRDs with an R343V or R343I substitution have increased mannan binding activity and greatly increased antiviral activity.
Result: As in the case of mAb 246-02, the binding of 3C3-C-20 was greatly diminished by the
Recognition of mannosylated ligands and influenza A virus by human surfactant protein D: contributions of an extended site and residue 343.
Abstract: A mutant with valine at 343 (R343V) showed enhanced binding to mannan relative to wild type and R343A.
Abstract: Although hNCRDs show negligible binding to influenza A virus (IAV), R343V showed markedly enhanced viral neutralizing activity.
Abstract: Both proteins showed efficient recognition of linear and branched subdomains of high-mannose glycans on carbohydrate microarrays, and R343V showed increased binding to a subset of the oligosaccharides.
Abstract: Crystallographic analysis of an R343V complex with 1,2-DM showed a novel mode of binding.
Introduction: Our experiments demonstrate greatly enhanced anti-viral activity of R343V associated with utilization of a modified carbohydrate binding site for alpha1-2 linked mannoses, which are commonly
IV mutation literature information.
PMID: 
2014
American journal of physiology. Lung cellular and molecular physiology
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