Disease relevance of P97

• The C-terminal portion, including two repeat regions, R1 and R2, of the P97 adhesin of Mycoplasma hyopneumoniae strain E-1 was successfully translocated and expressed on the E. rhusiopathiae YS-1 cell surface after it was fused to SpaA.1, a cell surface protective antigen of E. rhusiopathiae [1].
• Both recombinant P97 protein expressed in an Escherichia coli opal suppressor host and M. hyopneumoniae bound specifically to swine cilia, and the binding was inhibited by heparin and fucoidan, thus supporting the hypothesis that P97 was actively involved in binding to swine cilia in vivo [2].
• The attenuated Erysipelothrix rhusiopathiae YS-19 strain was constructed for the purpose of delivering the C-terminal portion of the Mycoplasma hyopneumoniae P97 adhesin to the mucosal surface of the respiratory tract of pigs [3].
• Vaccine efficacy of the attenuated Erysipelothrix rhusiopathiae YS-19 expressing a recombinant protein of Mycoplasma hyopneumoniae P97 adhesin against mycoplasmal pneumonia of swine [3].

High impact information on P97

• M. hyopneumoniae adheres to and adversely affects the function of ciliated epithelial cells of the respiratory tract, and the cilium adhesin (Mhp183, P97) is intricately but not exclusively involved in this process [4].
• The P97 adhesin and P102 genes of Mycoplasma hyopneumoniae each have six paralogs in the genome [5].
• Molecular analysis of the P97 cilium adhesin operon of Mycoplasma hyopneumoniae [6].
• Further analysis of the DNA sequences surrounding the P97 structural gene revealed an operon composed of two ORFs, P97 and one coding for a 102.3-kDa protein designated P102 [6].
• The disease process is initiated by adherence of M. hyopneumoniae to the cilia of swine respiratory epithelium through an interaction involving P97, a surface-associated protein, and cilia-specific receptors [6].

Chemical compound and disease context of P97

• The objective of this study was to develop and to evaluate in BALB/c mice a recombinant subunit vaccine (rLTBR1) containing the R1 region of P97 adhesin of M. hyopneumoniae (R1) fused to the B subunit of the heat-labile enterotoxin of Escherichia coli (LTB). rLTBR1 formed functional oligomers that presented high affinity to GM1 ganglioside [7].

Biological context of P97

• These studies showed that the cilium binding site was located in the AAKPV(E) repeat sequence of P97, referred to as the R1 repeat [8].
• The gene coding for P97 was then identified by Tn1000 mutagenesis of recombinant clones [2].
• Hybridization analysis and subcloning experiments showed that the P97 adhesin-encoding gene was present as a single copy in the M. hyopneumoniae chromosome [6].
• Comparison of the three M. hyopneumoniae adhesin genes revealed that the genes encoding P97 and Mhp1, and the strain J gene encoding the 94 kDa antigen contained 15, 12 and 9 tandem repeats, respectively, in RR1, and 4, 5 and 5 tandem repeats, respectively, in RR2 [9].
• AFLP (>0.99) and PCR-RFLP of the P146 encoding gene (>0.98) were more discriminatory than RAPD (0.95) and estimation of the VNTR of P97 (<0.92) [10].

Anatomical context of P97

• This interaction involves an adhesin called P97; the cilium binding activity of this protein was localized to the carboxy terminus, which included two repeat regions, R1 and R2 (T. Hsu, S. Artiushin, and F. C. Minion, J. Bacteriol. 179:1317-1323, 1997) [8].

Analytical, diagnostic and therapeutic context of P97

• A protein chip based on surface plasmon resonance (SPR) was developed for measuring the Mycoplasma hyopneumoniae antibody titres using a recombinant 30-kDa fragment of P97 adhesin as an antigen [11].

References