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Literature DB >> 10526185

The conserved undecapeptide shared by thiol-activated cytolysins is involved in membrane binding.

T Jacobs¹, M D Cima-Cabal, A Darji, F J Méndez, F Vázquez, A A Jacobs, Y Shimada, Y Ohno-Iwashita, S Weiss, J R de los Toyos.

Abstract

Thiol-activated cytolysins share a conserved hydrophobic, Trp-rich undecapeptide that is suggested to be involved in membrane binding and intercalation. The neutralizing monoclonal antibody PLY-5 recognizes all members of this toxin family and peptide mapping assigned its epitope to the undecapeptide motif. This antibody inhibited binding of the toxins to host cell membranes and the epitope was no longer available for binding when a preformed toxin/membrane complex was tested. These results confirm the model of cytolysin binding suggested by structural data.

Entities: Chemical Gene

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Year: 1999 PMID： 10526185 DOI： 10.1016/s0014-5793(99)01297-1

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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Cited

20 in total

10. Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.

Authors: Casie E Soltani; Eileen M Hotze; Arthur E Johnson; Rodney K Tweten
Journal: Proc Natl Acad Sci U S A Date: 2007-12-12 Impact factor: 11.205

The conserved undecapeptide shared by thiol-activated cytolysins is involved in membrane binding.

1. Rapid and sensitive detection of Listeria monocytogenes by loop-mediated isothermal amplification.

2. Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins.

Review 3. Membrane assembly of the cholesterol-dependent cytolysin pore complex.

4. Identification of invasive serotype 1 pneumococcal isolates that express nonhemolytic pneumolysin.

5. Rapid purification of recombinant listeriolysin O (LLO) from Escherichia coli.

6. Histone modifications induced by a family of bacterial toxins.

7. The aromatic ring of phenylalanine 334 is essential for oligomerization of Vibrio vulnificus hemolysin.

8. The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin.

9. Protection against pneumococcal pneumonia in mice by monoclonal antibodies to pneumolysin.

10. Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.