4.2 Article

Bactericidal Activity Identified in 2S Albumin from Sesame Seeds and In silico Studies of Structure-Function Relations

Journal

PROTEIN JOURNAL
Volume 30, Issue 5, Pages 340-350

Publisher

SPRINGER
DOI: 10.1007/s10930-011-9337-x

Keywords

Antimicrobial proteins; 2S albumins; Phylogenetic analysis; Homology modeling; Structure-function relationship

Funding

  1. CAPES
  2. CNPq
  3. FAPDF
  4. FAPEMIG
  5. UCB

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Pathogenic bacteria constitute an important cause of hospital-acquired infections. However, the misuse of available bactericidal agents has led to the appearance of antibiotic-resistant strains. Thus, efforts to seek new antimicrobials with different action mechanisms would have an enormous impact. Here, a novel antimicrobial protein (SiAMP2) belonging to the 2S albumin family was isolated from Sesamum indicum kernels and evaluated against several bacteria and fungi. Furthermore, in silico analysis was conducted in order to identify conserved residues through other 2S albumin antimicrobial proteins (2S-AMPs). SiAMP2 specifically inhibited Klebsiella sp. Specific regions in the molecule surface where cationic (RR/RRRK) and hydrophobic (MEYWPR) residues are exposed and conserved were proposed as being involved in antimicrobial activity. This study reinforces the hypothesis that plant storage proteins might also play as pathogen protection providing an insight into the mechanism of action for this novel 2S-AMP and evolutionary relations between antimicrobial activity and 2S albumins.

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