1.C.109 The Bacterial Hemolysin A (B-Hemolysin A) Family
The hemolysins of Serpulina (Brachyspira) hyodysenteriae are active at 27 to 40
degrees C and pH 3 to 9 and are unaffected by enzymatic inhibitors. Pore
formation was demonstrated by the inhibition of hemolysis with
molecules of 2.0 to 2.3 nm in diameter and the release of 86Rb from erythrocytes without hemoglobin release after exposure to native hemolysin (Hyatt and Joens 1997).
This family belongs to the .
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Hemolysin A, TlyA of 240 aas
TlyA of Brachyspira (Serpulina) hyodysenteriae
S-Hemolysin of 271 aas (Rajesh et al. 2013).
S-Hemolysin of Streptomyces coelicolor
Putative hemolysin of 253 aas, TlyA. In one study hemolysin activity was not detected, but adhsion to Caco cells was demonstrated (Sałamaszyńska-Guz and Klimuszko 2008).
TlyA of Campylobacter jejuni
Hemolysin and RNA methyltransferase of 268 aas, TlyA (Rahman et al. 2010; Monshupanee 2013). The assignment of this protein as an hemolysin has be questioned (Arenas et al. 2011).
TlyA of Mycobacterium tuberculosis
Haemolysin III, TlyA family member of 279 aas (Ramarao and Sanchis 2013).
Haemolysin of Bacillus cereus
The 'non-conventional' hemolysin, TlyA, a pore-forming hemolysin with potent
cytotoxic activity, is of 235 aas (Javadi and Katzenmeier 2016). It causes agglutination, fusion and permeability of synthetic
liposome vesicles. Agglutination activity could also be observed
with erythrocytes before the induction of its pore-forming hemolytic
TlyA also induces disruption of liposome membranes (Lata and Chattopadhyay 2014).
TlyA of Helicobacter pylori