Aeromonas

In otlier reeent papers we exploit a piezoeleetrie deviee by immobilizing a speeifie sequenee of bases of the patlrogen mieroorganism Aeromonas belonging to the gene eodifying for the formation of the toxin Aerolysin. 

Aeromonas ean be present in water, milk, eheese, in iee eream, in sausages ete. 

Amphibians. Immunosuppression has been shown to occur during metamorphosis in several amphibians, and appears to be hormonally regulated. The disappearance of 11 populations of toad from Colorado was associated with immune suppression, and frog mortalities have been associated with infection by a commonly occurring bacteria, Aeromonas hydrophila the cause of the immunosuppression in these animals has not been elucidated. " ... 

Aeromonas hydrophila is a bacterium that causes diarrheal diseases and deep wound infections. These complications arise due to pore formation in sensitive cells by the protein toxin aerolysin. Proteolytic processing of the 52-kD precursor proaerolysin (Figure 10.34) produces the toxic form of the protein, aerolysin. Like a-hemolysin, aerolysin monomers associate to form a heptameric transmembrane pore. Michael Parker and coworkers have proposed... 

FIGURE 10.34 The structure of proaerolysiu, produced by Aeromonas hydrophila. 

Parker, M., Buckley, J., Postma, J., et al., 1994. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 367 292-295. 

S,3S)-Dicarboxyaziridine (112) was isolated from a Streptomyces strain in 1975 and found to have moderate antibacterial activity against Aeromonas salmonecida [176]. Subsequent studies showed that 112 acts as a competitive inhibitor of fumar-ase, through mimicry of a carbanionic transition state [177]. No biosynthetic studies have been reported for 112, but it is conceivable that it may arise from cydiza-tion of (3R)-hydroxyaspartic acid (Figure 11.18). 

Class B Metallo p-lactamases L1 enzyme of S. maltophilia enzyme of Aeromonas spp. CcrA enzyme found in 1-3% of 8. fragilis isolates. All enzymes are carbapenemases IMP, VIM and SPM type carbapenemases... 

Class D Serine p-lactamases OXA enzymes (oxacillinases) of Acinetobac-ter spp. and some Aeromonas spp. Some OXA enzymes are carbapenemases Most OXA types are chromosomal... 

Studies on S-layers present on the cell envelopes of a great variety of pathogenic organisms [100] revealed that these crystalhne arrays can represent important virulence factors. Most detailed studies have been performed on the fish pathogenic bacteria Aeromonas salmonicida and Aeromonas hydrophila [102] and the human pathogen Campylobacter fetus uh p. fetus [103] and Bacillus anthracis [104]. For example, whole-cell preparations or partially purified cell products are currently used as attenuated vaccines against various fish pathogens [102,105]. 

Three 3-amino-3,6-dideoxyhexoses, having the d- and L gluco and D-ga-lacto configurations, have been found. The two D-sugars are not very common, but occur in some 0-antigens for example, those from E. coli 0114 (Ref. 60) and E. coli 02 (Ref 61), respectively. The D-galacto isomer has also been found in the cell-wall polysaccharide from Eubacterium saburreum strain L13.3-Amino-3,6-dideoxy-L-glucose has been found in the core part of the Aeromonas hydrophila chemotype 111 LPS. 

Aeromonas species producing sodium channel blockers, 80r,82 Agelas dispar, 320... 

Kiyohara H, K Nagao, R Nomi (1976) Degradation of phenanthrene through o-phthalate by an Aeromonas sp. Agric Biol Chem 40 1075-1082. 

Van der Kooij D, A Visser, JP Oranje (1980) Growth of Aeromonas hydrophila at low concentrations of substrates added to tap water. Appl Environ Microbiol 39 1198-1204. 

Similar to catechins, several studies have reported that proanthocyanidins exhibit a more or less pronoimced antibacterial activity. Chimg et al. [76] reported that proanthocyanidins determine the growth inhibition of strains of Aeromonas spp.. Bacillus spp., Clostridium botulinum, Clostridium per-fringens, Enterobacter spp., Klebsiella spp., Proteus spp.. Pseudomonas spp.. Shigella spp., S. aureus. Streptococcus spp., and Vibrio spp. 

Many rhizobacteria are classified as chitinolytic and, for example, Serratki marsescens, which excretes chitinase, was found to be an effective biocontrol agent against Sclerotium rolfsii (135). Similarly, Aeromonas caviae was found to reduce disease caused by Rhizoctonia solani, Fusarium oxysporuin, and Sclerotium rolfsii (136). There is also evidence to support the role of P-l,3 glucanase in biocontrol of soil-borne plant pathogens (137). 

J. Inbar and I. Chet, Evidence that chitinase produced by Aeromonas caviae is, involved in the biological control of soil-borne plant pathogens by this bacteria. Sod Biology and Biochemistry 23 913 (1991). 

Figure 5.6 Successful transformation of Aeromonas hydrophila raw spectra A acquired on day 27 to new locations a (relationship indicated with a dotted arrow) near an A. hydrophila day 1 library spectrum C using another day 27 bacterium, E. coli 1090 D as reference compared to its own day 1 E. coli 1090 Library spectrum L (relationship indicated with a solid arrow).

There are only very few PHA synthases which can incorporate 3HASCL as well as 3HAmcl into the accumulated PHAs. Examples are the PHA synthases of T. pfennigii and Aeromonas caviae, which synthesize, for example, copolyesters of 3HB, 3HHx plus 3HO [26], or of 3HB plus 3HHx [59], from fatty acids, respectively. Recently it was found that the type I-PHASCL synthase of R. eutropha also conferred the incorporation of 3HHx [60] or of 3HO plus 3HD [61] into PHAs in addition to 3HB to certain recombinant strains of enterobacteria. 

Rhodospirillum rubrum Ha - Rhodospirillum rubrum ATCC 25903 —Acinetobacter sp. RA3849 —Aeromonas caviae FA440 —Rhodobacter sphaeroides... 

In Aeromonas caviae, 3-ketothiolase and acetoacetyl-CoA reductase are absent. In this species, the synthesis of poly(3HB) proceeds via an enoyl-CoA hy-dratase from either crotonyl-CoA or hexenoyl-CoA. The enoyl-CoA derivatives stem from the fatty-acid oxidation pathway [18]. 

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