Molecular genetics and pathogenesis of Clostridium perfringens

Abstract

Clostridium perfringens is the causative agent of a number of human diseases, such as gas gangrene and food poisoning, and many diseases of animals. Recently significant advances have been made in the development of C. perfringens genetics. Studies on bacteriocin plasmids and conjugative R plasmids have led to the cloning and analysis of many C. perfringens genes and the construction of shuttle plasmids. The relationship of antibiotic resistance genes to similar genes from other bacteria has been elucidated. A detailed physical map of the C. perfringens chromosome has been prepared, and numerous genes have been located on that map. Reproducible transformation methods for the introduction of plasmids into C. perfringens have been developed, and several genes coding for the production of extracellular toxins and enzymes have been cloned. Now that it is possible to freely move genetic information back and forth between C. perfringens and Escherichia coli, it will be possible to apply modern molecular methods to studies on the pathogenesis of C. perfringens infections.

NetF-producing Clostridium perfringens and its associated diseases in dogs and foals

“…Most, such as collagenase (κ-toxin), neuraminidase, caseinase (λ-toxin), deoxyribonuclease (η-toxin), hyaluronidase (μ-toxin), and urease, have individually only a minor role in the pathogenesis of C. perfringens diseases, but their cumulative effect is likely profound. 58,59 The primary and cumulative role of these and other degradative enzymes is the generalized degradation of host tissues to provide the essential nutrients that the organism itself is incapable of producing. 59 However, further work is required to elucidate the contributions of these exoenzymes to C. perfringens virulence.…”

“…58,59 The primary and cumulative role of these and other degradative enzymes is the generalized degradation of host tissues to provide the essential nutrients that the organism itself is incapable of producing. 59 However, further work is required to elucidate the contributions of these exoenzymes to C. perfringens virulence. For instance, it has been reported that C. perfringens exo-alpha-sialidase, NanI, is able to increase the binding capacity of some toxins, including CPB, CPE, and ETX, to the host cell membrane and therefore enhances their cytotoxicity.…”

Maternal effects on early-life gut microbiome maturation in a wild nonhuman primate

“…The early-life microbiome of geladas was also characterized by a high number of potentially pathogenic bacteria known to cause enteric infection in human newborns and captive animals (Clostridioides, Helicobacter, Clostridium) [87][88][89][90][91] and several bacterial groups involved in the activation of the host immune system such as butyrate-producing (Blautia, Faecalibacterium, Butyricicoccus, Butyricimonas) and mucin-degrading bacteria (Akkermansia, Ruminococcus gnavus and R. torques). Collectively, this microbial profile suggests that immune function is a priority for gelada infants.…”

“…Interestingly, cluster 1 also included several putatively pathogenic genera (Figure 3B), including some bacterial species most responsible for enteric infections and diarrheal diseases in human newborns and captive animals (e.g., Clostridioides difficile, Helicobacter macacae, Clostridium butyricum, C. perfringens [87][88][89][90][91]) (Table S7). It also included 3 major groups of mucin-degrading bacteria (Akkermansia, [Ruminococcus] gnavus group and [Ruminococcus] torques) (Figure 3C) that are involved in the development of the intestinal mucosa, a primary line of immune defense [92].…”

A naturally occurring point mutation in the hyaluronidase gene (hysA1) of Staphylococcus aureus UAMS-1 results in reduced enzymatic activity

“…The hyaluronidases are a group of naturally-occurring enzymes that degrade hyaluronic acid and can be classified into one of three categories depending upon their source; mammalian, venom, or microbial (Girish and Kemparaju 2007). The bacterial hyaluronidases (also referred to as hyaluronate lyase) have been shown to contribute to infection from a number of different bacterial species; it has been proposed that by degrading the polymer in the extracellular matrix of the host, bacterial pathogens may enhance contact with host cell constituents and facilitate dissemination of bacterial cells and toxins throughout the host (Smith 1979a;Rood and Cole 1991;Cheng et al 1995;Hynes and Walton 2000;Senn et al 2005;Starr and Engleberg 2006). In addition, the bacterial pathogen may utilize the degraded polymer product as a suitable energy source (Smith 1979b;Fitzgerald and Repesh 1987;Pettersson et al 1996;Homer et al 1997;Shain et al 1997;Starr and Engleberg 2006).…”