Edwardsiella Tarda On Blood Agar

Fig. 7. HEp2 cells invaded by E. tarda, magnification x 200.

1991b; Ling et al., 2000). Subsequently, two p-hemolysins from E. tarda have been cloned and sequenced. The first, cloned from strain ET16, resides in an open-reading frame (ORF) of ~933

bp encoding for a 311 amino acid polypeptide with a molecular mass of 34 kDa (Chen et al., 1996). The structural gene for this P-hemolysin shares over 90% homology to the hemolysin BL of Bacillus cereus (Hirono et al., 1997). The frequency of this gene in E. tarda isolates is unknown. A second P-hemolysin from E. tarda strain MZ8901 has been cloned and sequenced by Hirono et al. (1997). The gene, designated ethA, resides in an ORF of 4,782 bp that encodes for a 165.3 kDa product. The deduced amino acid sequence of EthA shares the highest degree of homology (47%) with the ShlA hemolysin of Serratia marcescens (Hirono et al., 1997). All 72 E. tarda strains tested reacted with an ethA probe, indicating that this appears to be the predominant P-hemolysin carried by most isolates. A study by Strauss et al. (1997) found that a transposon-mutagenized strain of E. tarda is noncytotoxic and defective for hemolysin production (Fig. 8) and is also unable to enter Hep-2 cells. This hemolysin appears to be very similar or identical to that described by Hirono et al. (1997). This implies that both hemolytic and invasive capabilities of edwardsiellae are linked

Image Edwardsille Turda Blood Agar
Fig. 8. Wild type (WT) E. tarda and a nonhemolytic mutant (hly ) of E. tarda on blood agar. (From Strauss et al., 1997, with permission)

Fig. 9. Deferrated L agar seeded with E. tarda with sterilized suspensions of transferrin, hemin, ferritin, protoporphyrin IX, hemoglobin and hematin (clockwise, starting at 1 o'clock) added to individual wells. In this iron-starved medium, growth of E. tarda occurred only in the presence of hemin, hemoglobin and hematin.

Fig. 9. Deferrated L agar seeded with E. tarda with sterilized suspensions of transferrin, hemin, ferritin, protoporphyrin IX, hemoglobin and hematin (clockwise, starting at 1 o'clock) added to individual wells. In this iron-starved medium, growth of E. tarda occurred only in the presence of hemin, hemoglobin and hematin.

together. The hemolysin is also regulated by the availability of iron (Janda and Abbott, 1993; Fig. 9).

Elevated levels of hemolysin are produced by E. tarda strains under iron-limited conditions and two putative ferric uptake regulator (Fur) binding sites are on the 5' upstream region of the activation/secretion protein gene ethB overlapping the promoter region and ribosome-binding site (Janda and Abbott, 1993; Hirono et al., 1997). Thus expression is upregulated under iron-limited conditions and downregulated in the presence of an excess of iron.

A heat-stable (60°C, 30 min; 100°C, 15 min) enterotoxin has been detected in 3 of 25 E. tarda strains employing the rabbit ligated ileal loop assay (Bockemuhl et al., 1983). This enterotoxin did not cause Chinese hamster ovary (CHO) cell elongation. Conceivably, this enterotoxin could be operative in cases of secretory diarrhea associated with E. tarda. Also, E. tarda has recently been shown to induce plasma membrane ruffling in HEp-2 cells, a phenomenon that does not correlate with adhering bacteria (Phillips et al., 1998). The authors suggest that this may involve a distinct pathogenic mechanism in E. tarda.

A number of other potential virulence factors have been identified in E. tarda strains. These include hemagglutinins, dermatonecrotic substances, siderophores, and resistance to complement-mediated lysis (Ullah and Arai, 1983; Wong et al., 1989; Janda et al., 1991a). Their possible role in pathogenicity is speculative at present.

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Prokaryotes (2006) 6:90-98 DOI: 10.1007/0-387-30746-x_5

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