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An intimate link between antimicrobial peptide sequence diversity and binding to essential components of bacterial membranes ArchiMer
Schmitt, Paulina; Rosa, Rafael D.; Destoumieux-garzon, Delphine.
Antimicrobial peptides and proteins (AMPs) are widespread in the living kingdom. They are key effectors of defense reactions and mediators of competitions between organisms. They are often cationic and amphiphilic, which favors their interactions with the anionic membranes of microorganisms. Several AMP families do not directly alter membrane integrity but rather target conserved components of the bacterial membranes in a process that provides them with potent and specific antimicrobial activities. Thus, lipopolysaccharides (LPS), lipoteichoic acids (LTA) or the peptidoglycan precursor Lipid II are targeted by a broad series of AMPs. Studying the functional diversity of immune effectors tells us about the essential residues involved in AMP mechanism of...
Tipo: Text Palavras-chave: Functional diversity; Defensin; Anti-lipopolysaccharide factor; Mechanism of action; Resistance.
Ano: 2016 URL: http://archimer.ifremer.fr/doc/00286/39710/38165.pdf
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