Characterization of pyruvate dehydrogenase subunit B and enolase as plasminogen-binding proteins in Mycoplasma pneumoniae.

摘要: The obligate pathogenic mycoplasma species Mycoplasma pneumoniae uses a limited but effective repertoire of virulence factors to infect and colonize the human respiratory tract. Besides development unique adhesion complex expression tissue-damaging factors, surface-located glycolytic enzymes their capacity bind components extracellular matrix (ECM) support pathogen–host interactions. Here, we demonstrated that enolase (Mpn606) pyruvate dehydrogenase subunit B (Mpn392; PDHB) M. show concentration-dependent binding plasminogen. Monospecific polyclonal antisera against both recombinant proteins reduced plasminogen significantly. surface location PDHB not was using Triton X fractionation total protein content, membrane fractionation, colony blotting, mild proteolysis cells, immunofluorescence tests. To characterize site in surface-displaced PDHB, mycoplasmal separated into four followed by investigation behaviour peptides overlap part interacting with Spot analysis resulted novel region 12 amino acids (FPAMFQIFTHAA, position 91 102 PDHB), which is responsible exclusively for also interacts dose-dependent manner this host protein. data indicate plasminogen-binding especially surface-associated may contribute pathogenesis infections.