Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4359431 | Research in Microbiology | 2006 | 6 Pages |
Abstract
We characterised pneumococcal neuraminidase A (NanA) by determining key amino acids required for the enzymatic activity of the protein. Single replacement of two residues, hypothesised to be important for the catalytic activity of neuraminidases, resulted in total loss of activity (E647 with Q or Y752 with F). The mutation of R663 to H caused substantial reduction in the catalytic ability of the enzyme. The inactive neuraminidases thus produced were protective immunogens against pneumococcal pneumonia in mice.
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