Enzymatically active Peptostreptococcus magnus: association with site of infection

Abstract

Fifty-four strains of Peptostreptococcus magnus (11 were recovered from abdominal infections, 18 were from nonpuerperal breast abscesses, and 21 were from diabetic foot infections; the type strain and three other strains were from the American Type Culture Collection, Rockville, Md.) and the type strain of Peptostreptococcus micros were tested for their ability to produce various enzymes, including catalase, hippurate hydrolase, serine dehydratase, threonine dehydratase, collagenase, gelatinase, alkaline phosphatase, and esterase C4. The data were analyzed by cluster analysis. The results showed that all but one strain could be assigned to either of two distinct, valid clusters. The first cluster of 11 strains was composed of strains that were relatively inactive, having produced one or two of the eight strain-dependent enzymes. The second was a large cluster of strains (n = 43) that were considerably more active, all having produced at least three enzymes; the vast majority of strains (89%o) produced four or more enzymes. The unclustered strain produced one enzyme that was different from that produced by the strains in the first cluster. The x2 test of homogeneity applied to the clustering solution indicated that greater enzyme activity was significantly associated with the site of infection (P < 0.001). The more enzymatically active P. magnus strains were recovered significantly more often from nonpuerperal breast abscesses and diabetic foot infections than they were from abdominal infections. These results may provide insight into the nature of certain polymicrobial soft tissue infections and suggest that (i) P. magnus may participate more in nonpuerperal breast and diabetic foot infections than in abdominal infections and that (ii) peptostreptococcal production of proteolytic enzymes may have an important adjunctive effect on the pathogenesis of certain soft tissue infections.

Gram-positive anaerobic cocci – commensals and opportunistic pathogens

“…All strains produce ammonia from glycine and most strains produce ammonia from threonine and serine . Aminopeptidase activities have been reported (Ng et al, 1998) and also catalase activity (Murdoch & Mitchelmore, 1991;Krepel et al, 1992). Coagulase, indole and urease are not formed, and no strain reduces nitrate Murdoch, 1998).…”

“…Typical infections connected with F. magna are soft-tissue abscesses, wound infections, bone and prosthetic joint infections (Fitzgerald et al, 1982;Davies et al, 1988;Murdoch, 1998;Brook & Frazier, 2000;Brazier et al, 2008;Brook, 2008;Holst et al, 2008;Levy et al, 2009;Martin et al, 2009). The bacterium has also been described in septic arthritis (Fitzgerald et al, 1982;Hunter & Chow, 1988), nonpuerperal breast abscesses (Edmiston et al, 1990;Krepel et al, 1992;Castello et al, 2007) and in vaginoses (Kastern et al, 1990;Ricci et al, 2001;Aggarwal et al, 2003). In addition, rare cases of infectious endocarditis on prosthetic valves (Cofsky & Seligman, 1985;Pouëdras et al, 1992;van der Vorm et al, 2000;Bassetti et al, 2003;Fournier et al, 2008) and postoperative mediastinitis (Kernéis et al, 2009) caused by F. magna have been described.…”

“…However, the proteins responsible for these actions have not yet been identified. Finegoldia magna strains with enhanced collagenase, gelatinase and hippurate hydrolase activity have been isolated from nonpuerperal abscesses and diabetic foot infections (Krepel et al, 1991(Krepel et al, , 1992. Furthermore, supernatant from strains isolated from chronic leg ulcers inhibited keratinocyte wound repopulation and endothelial tubule formation in vitro (Stephens et al, 2003).…”

Potential role of anaerobic cocci in impaired human wound healing

“…Interestingly, GPAC produce a range of hydrolytic enzymes including hyaluronidase, gelatinase, and collagenase 27 . 51, 52 This finding may suggest not only direct enhancement of extracellular matrix (ECM) turnover, but also indirect potentiation of a chronic inflammatory response (Figure 1). The production of hydrolytic enzymes by the GPAC is not a universal phenotype and varies between strains and between disease sites 53 .…”

Identification of molecular mechanisms used by Finegoldia magna to penetrate and colonize human skin

“…Another important virulence factor of F. magna is the subtilase-like enzyme SufA, which protects the bacterium from antibacterial activities of LL-37, histones and MIG/ CXCL9 by proteolytic degradation (Karlsson et al, 2007;Murphy and Frick, 2013). F. magna also has the capability to produce a capsule and the enzymes collagenase and gelatinase, which could be other important pathogenicity factors (Brook, 1986;Krepel et al, 1992).…”