High-affinity interaction between fibronectin and the group B streptococcal C5a peptidase is unaffected by a naturally occurring four-amino-acid deletion that eliminates peptidase activity.
Tamura, Glen S
High-affinity interaction between fibronectin and the group B streptococcal C5a peptidase is unaffected by a naturally occurring four-amino-acid deletion that eliminates peptidase activity. [electronic resource] - Infection and immunity Oct 2006 - 5739-46 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
0019-9567
10.1128/IAI.00241-06 doi
Adhesins, Bacterial--chemistry
Amino Acid Sequence
Endopeptidases--chemistry
Fibronectins--chemistry
Genetic Complementation Test
Recombinant Proteins--chemistry
Sequence Deletion
Streptococcus agalactiae--enzymology
Surface Plasmon Resonance
High-affinity interaction between fibronectin and the group B streptococcal C5a peptidase is unaffected by a naturally occurring four-amino-acid deletion that eliminates peptidase activity. [electronic resource] - Infection and immunity Oct 2006 - 5739-46 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
0019-9567
10.1128/IAI.00241-06 doi
Adhesins, Bacterial--chemistry
Amino Acid Sequence
Endopeptidases--chemistry
Fibronectins--chemistry
Genetic Complementation Test
Recombinant Proteins--chemistry
Sequence Deletion
Streptococcus agalactiae--enzymology
Surface Plasmon Resonance