The amino acid sequence of a gonococcal growth inhibitor from Staphylococcus haemolyticus

Abstract

A gonococcal inhibitor produced by Staphylococcus haemolyticus was separated into three components by reverse-phase h.p.l.c. The amino acid composition analysis of each of the three components indicated extensive similarities. N-Terminal sequence analysis of all three components allowed the identification of the first 27-30 residues of each. The complete primary structure of each component was determined from the sequence analysis of trypic peptides and peptides generated by mild acid hydrolysis. Each component is composed of 44 amino acid residues, with evidence suggesting the presence of an N-terminal formylmethionine residue in each. The components I, II and III have respectively 33, 29 and 33 identical amino acid residues in their sequences, which represents 75 %, 65.9 % and 75 % homology. These components contain a high proportion of hydrophobic amino acids, and their hydrophobicity profiles are closely related. Also, each of the three components contains a positively charged residue (lysine) as the third residue, followed by a core of hydrophobic residues. These results suggest that the three components are possible signal sequences of one or more secreted or membrane-associated proteins.

Class II antimicrobial peptides from lactic acid bacteria

“…These latter peptides are referred to as the SLUSH A, B, and C , produced by Staphylococcus lugdunensis, and AGS-1, -2, and -3, produced by Staphylococcus haemolyticus. [63][64][65] These peptides are also synthesized ribosomally, but they lack a leader sequenc, and furthermore, no immunity gene is cotranscribed. In contrast to the SLUSH and AGS systems, enterocin L50 is only bactericidal and not hemolytic.…”

Activity ofStaphylococcus epidermidisPhenol‐Soluble Modulin Peptides Expressed inStaphylococcus carnosus

“…High-performance liquid chromatography (HPLC) isolated 3 of the components, designated PSMa, PSMb, and PSMg, which, according to the results of amino-acid sequence analysis and identification and sequencing of their genes, were found to be polypeptides of 22, 44, and 25 aa, respectively [1]. PSMa (fMADVIAKIVEIVKGLIDQFTQK) had no close homology, according to the results of a standard BLAST (available at: http://www.ncbi.nih.gov/BLAST/) search, although some similarity to PSMg (d-toxin) was observed, PSMb (fMSKLAEAIANTVKAAQDQDWTKLGTSIVDIVESG-VSVLGKIFGF) had sequence homology of 35%-73% to previously described polypeptides from Staphylococcus hemolyticus [7] and Staphylococcus lugdunensis [8], and PSMg (fMAADIIS-TIGDLVKWIIDTVNKFKK) had complete sequence homology to S. epidermidis d-toxin [9]. The structure of the fourth component, with a mass of 2648 Da, was not determined [1].…”

Staphylococcus epidermidis surfactant peptides promote biofilm maturation and dissemination of biofilm-associated infection in mice

“…It is therefore important to stress that, in contrast, our results indicate that the PSM-based surfactant detachment mechanism is largely independent of the biofilm matrix chemical composition. Finally, presence of PSMs and PSM-like molecules in many staphylococci including S. aureus (18,37,38) indicates that PSMs may also contribute to biofilm structuring in other staphylococcal species, which remains to be investigated.…”