Crystallization of Sendai virus HN protein complexed with monoclonal antibody Fab fragments.
The hemagglutinin-neuraminidase (HN) protein of Sendai virus has been isolated from virus particles in a biologically active soluble form after removal by proteolytic digestion of the hydrophobic amino-terminal anchor sequence (S. D. Thompson, W. G. Laver, K. G. Murti, A. Portner, J. Virol., 62, 4653-4660, 1988). The soluble HN exists as both dimers and tetramers, and crystallization trials with each of these forms have so far yielded amorphous material. Dimers complexed with Fab fragments of a monoclonal antibody formed long needle crystals. So far, these are not suitable for X-ray diffraction analysis but the results suggest that HN molecules from paramyxoviruses, even if not crystallizable, may, when complexed with Fab fragments, in some cases yield crystals suitable for X-ray diffraction analysis.
Laver
W G
WG
John Curtin School of Medical Research, Australian National University, Canberra.
Thompson
S D
SD
Murti
K G
KG
Portner
A
A
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral / Q000276:immunology; D000936:Antigen-Antibody Complex; D003461:Crystallography; D015707:HN Protein; D006389:Hemagglutinins, Viral / Q000276:immunology*; D007140:Immunoglobulin Fab Fragments; D008854:Microscopy, Electron; D010222:Parainfluenza Virus 1, Human / Q000276:immunology*; D014759:Viral Envelope Proteins / Q000276:immunology* / Q000648:ultrastructure
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D000936:Antigen-Antibody Complex; D015707:HN Protein; D006389:Hemagglutinins, Viral; D007140:Immunoglobulin Fab Fragments; D014759:Viral Envelope Proteins