Article ID Journal Published Year Pages File Type
6136451 Microbial Pathogenesis 2011 6 Pages PDF
Abstract
► Mycoplasma gallisepticum α-enolase gene was expressed in Escherichia coli successfully. ► Purified recombinant enolase exhibited α-enolase catalytic activity. ► Immunoblotting and IFA identified α-enolase on the surface of M. gallisepticum cells. ► ELISA characterized recombinant enolase as a chicken plasminogen binding protein. Antiserum against M. gallisepticum α-enolase inhibited the adherence to DF-1 cells.
Keywords
Related Topics
Life Sciences Immunology and Microbiology Microbiology
Preview
The Mycoplasma gallisepticum α-enolase is cell surface-exposed and mediates adherence by binding to chicken plasminogen
Authors
, , , , , , ,