Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants.
The crystal structure of the N9 subtype neuraminidase of influenza virus was refined by simulated annealing and conventional techniques to an R-factor of 0.172 for data in the resolution range 6.0 to 2.2 A. The r.m.s. deviation from ideal values of bond lengths is 0.014 A. The structure is similar to that of N2 subtype neuraminidase both in secondary structure elements and in their connections. The three-dimensional structures of several escape mutants of neuraminidase, selected with antineuraminidase monoclonal antibodies, are also reported. In every case, structural changes associated with the point mutation are confined to the mutation site or to residues that are spatially immediately adjacent to it. The failure of antisera to cross-react between N2 and N9 subtypes may be correlated with the absence of conserved, contiguous surface structures of area 700 A2 or more.
CSIRO Division of Biomolecular Engineering, Parkville, Australia.
W R
WR
Tulip
J N
JN
Varghese
A T
AT
Baker
A
A
van Donkelaar
W G
WG
Laver
R G
RG
Webster
P M
PM
Colman
D000942:Antigens, Bacterial / Q000737:chemistry; D009980:Influenza A virus / Q000737:chemistry / Q000201:enzymology*; D008958:Models, Molecular; D009154:Mutation; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase / Q000737:chemistry* / Q000276:immunology; D011485:Protein Binding; D011487:Protein Conformation; D012794:Sialic Acids / Q000737:chemistry; D013499:Surface Properties; D013696:Temperature; D014961:X-Ray Diffraction
D000942:Antigens, Bacterial; D012794:Sialic Acids; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid