Marker exchange mutagenesis of the aerolysin determinant in Aeromonas hydrophila demonstrates the role of aerolysin in A. hydrophila-associated systemic infections

Chakraborty, Trinad; Huhle, B; Hof, Herbert; Bergbauer, H; Goebel, Werner

doi:10.1128/iai.55.9.2274-2280.1987

Cited by 97 publications

(44 citation statements)

References 22 publications

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“…Aerolysin/hemolysin is commonly found in A. hydrophila strains that cause bacteremia [26]. Additionally, it has been observed that deletion mutants for the aerA gene (encoding aerolysin) are less virulent than parental strains [27]. Our study demonstrated that the occurrence of the aerolysin/hemolysin genes in A. popo¤i (92%) is similar to that in common clinical species (e.g.…”

Section: Resultssupporting

confidence: 58%

Potential virulence and antimicrobial susceptibility of Aeromonas popoffii recovered from freshwater and seawater

Soler¹

2002

FEMS Immunology and Medical Microbiology

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Aeromonas popoffii is the most recent species within the genus Aeromonas described from freshwater. In our study this species was also recovered from this habitat and for the first time from seawater. Most of the virulence factors known in Aeromonas spp. (aerolysin/hemolysin, serine protease, lipases and DNases) were highly prevalent in this species. Third-generation cephalosporins and quinolones were the most active antimicrobial agents against A. popoffii.

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Section: Resultssupporting

confidence: 58%

Potential virulence and antimicrobial susceptibility of Aeromonas popoffii recovered from freshwater and seawater

Soler¹

2002

FEMS Immunology and Medical Microbiology

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“…This toxin binds to a specific glycoprotein receptor on the surface of eukaryotic cells, inserts into the lipid bilayer and aggregates to form holes, leading to the destruction of the membrane and to osmotic lysis (Howard and Buckley, 1982;Parker et al, 1994;Nelson et al, 1997). In a mouse toxicity model, an aerolysindeficient A. hydrophila mutant was less virulent than wild-type A. hydrophila (Chakraborty et al, 1987;Wong et al, 1998). An in vitro study demonstrated that aerolysin impairs epithelial integrity by promoting TJ protein redistribution (Buecker et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Aeromonas veronii and aerolysin are important for the pathogenesis of motile aeromonad septicemia in cyprinid fish

Ran

Qin

Xie

et al. 2018

Environmental Microbiology

124

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Aeromonas species are ubiquitous inhabitants of freshwater environments, and are responsible for fish motile aeromonad septicemia (MAS). A. hydrophila is implicated as the primary etiologic agent of MAS. Here, we analysed MAS epidemiological data for cyprinid fish in southern China, and found that A. veronii infections dominated. Consistent with this observation, A. veronii isolates were generally more virulent than A. hydrophila isolates when infecting germ-free zebrafish larvae via continuous immersion challenge. Through in vivo screening of the transposon library of the A. veronii strain Hm091, aerolysin was identified as the key virulence factor. Further results indicated that A. veronii Hm091 aerolysin disrupts the intestinal barrier of zebrafish, enabling systematic invasion by not only A. veronii Hm091 in a mono-infection, but also A. hydrophila NJ-1 in a mixed infection. Moreover, the differences in aerolysin expression and activity were the major contributor to the observed differences between the A. veronii and A. hydrophila strains regarding invasion efficacy via intestine. Together, our results provide new insights into the aetiology and pathogenesis of Aeromonas infections, and highlight the importance of A. veronii-targeted treatments in future efforts against MAS.

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“…The virulence of A. hydrophila is associated with the secretion of several extracellular proteins including aerolysin (Chakraborty et al, 1987), enterotoxin (Chakraborty et al, 1984), and protease (Leung and Stevenson, 1988). These extracellular proteins are secreted by a two-step pathway with the first step requiring the presence of a typical signal peptide so the extracellular protein can be translocated across the cytoplasmic membrane in a Sec-dependent manner (Wickner et al, 1991;Pugsley, 1993).…”

Section: Introductionmentioning

confidence: 99%

Cloning of an Aeromonas hydrophila type IV pilus biogenesis gene cluster: complementation of pilus assembly functions and characterization of a type IV leader peptidase/N‐methyltransferase required for extracellular protein secretion

Pepe

Eklund

Strom

1996

Molecular Microbiology

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Aeromonas hydrophila secretes several extracellular proteins that are associated with virulence including an enterotoxin, a protease, and the hole-forming toxin, aerolysin. These degradative enzymes and toxins are exported by a conserved pathway found in many Gram-negative bacteria. In Pseudomonas aeruginosa this export pathway and type IV pilus biogenesis are dependent on the product of the pilD gene. PilD is a bifunctional enzyme that processes components of the extracellular secretory pathway as well as a type IV prepilin. An A. hydrophila genomic library was transferred into a P. aeruginosa pilD mutant that is defective for type IV pilus biogenesis. The A. hydrophila pilD homologue, tapD, was identified by its ability to complement the pilD mutation in P. aeruginosa. Transconjugants containing tapD were sensitive to the type IV pilus-specific phage, PO4. Sequence data revealed that tapD is part of a cluster of genes (tapABCD) that are homologous to P. aeruginosa type IV pilus biogenesis genes (pilABCD). We showed that TapB and TapC are functionally homologous to P. aeruginosa PilB and PilC, the first such functional complementation of pilus assembly demonstrated between bacteria that express type IV pili. In vitro studies revealed that TapD has both endopeptidase and N-methyltransferase activities using P. aeruginosa prepilin as substrate. Furthermore, we show that tapD is required for extracellular secretion of aerolysin and protease, indicating that tapD may play an important role in the virulence of A. hydrophila.

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Marker exchange mutagenesis of the aerolysin determinant in Aeromonas hydrophila demonstrates the role of aerolysin in A. hydrophila-associated systemic infections

Cited by 97 publications

References 22 publications

Potential virulence and antimicrobial susceptibility of Aeromonas popoffii recovered from freshwater and seawater

Potential virulence and antimicrobial susceptibility of Aeromonas popoffii recovered from freshwater and seawater

Aeromonas veronii and aerolysin are important for the pathogenesis of motile aeromonad septicemia in cyprinid fish

Cloning of an Aeromonas hydrophila type IV pilus biogenesis gene cluster: complementation of pilus assembly functions and characterization of a type IV leader peptidase/N‐methyltransferase required for extracellular protein secretion

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