Insect Antimicrobial Peptides: Structures, Properties and Gene Regulation

Bulet, Philippe; Stöcklin, Reto

doi:10.2174/0929866053406011

Cited by 418 publications

(330 citation statements)

References 46 publications

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“…3. Cationic enriched with some specific amino acid residues (proline, arginine, phenylalanine, glycine and tryptophan), such as reported in the abaecins and apidaecins from honeybee hemolymph (Bulet and Stöcklin 2005).…”

mentioning

confidence: 85%

Peptides as toxins/defensins

Palma

2010

Amino Acids

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mentioning

confidence: 85%

Peptides as toxins/defensins

Palma

2010

Amino Acids

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“…CAMP inhibition by Pla at temperatures near 25°C might be important in the flea gut environment, which most likely includes CAMPs, as described for a variety of insects (8,11). Interestingly, the blood used to feed and infect fleas under laboratory conditions must contain high concentrations of Y. pestis (ϳ5 ϫ 10 8 CFU/ml) to achieve infection of a majority of fleas (25).…”

Section: Discussionmentioning

confidence: 99%

Capsular Antigen Fraction 1 and Pla Modulate the Susceptibility of Yersinia pestis to Pulmonary Antimicrobial Peptides Such as Cathelicidin

2008

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Inhaled Yersinia pestis produces a severe primary pneumonia known as pneumonic plague, which is contagious and highly lethal to humans and animals. In this study, we first determined the susceptibility of Y. pestis KIM6 to antimicrobial molecules of the airways. We found that (i) rat bronchoalveolar lavage fluid (rBALF) effectively killed KIM6 cells growing at 37°C; (ii) the antibacterial components of rBALF were small peptides (<10 kDa) that included two cationic antimicrobial peptides (CAMPs), the rat cathelicidin rCRAMP, and ␤-defensin RBD-1; (iii) the human cathelicidin LL-37 killed KIM6 cells as well as rBALF did; and (iv) the bactericidal property of LL-37 was synergistically amplified by human ␤-defensin 1, another constitutively expressed pulmonary CAMP. Second, the effects of three major surface proteins of Y. pestis, namely, the capsular antigen fraction 1 (F1), the pH 6 antigen (Psa fimbriae), and the outer membrane protease Pla, on the bactericidal effect of the antimicrobial rBALF peptides was determined with corresponding deletion mutants. We showed that (i) a Y. pestis psa mutant was only slightly more susceptible to rBALF than the parental KIM6 strain, (ii) a caf (F1 gene) mutant and a caf psa mutant were resistant to rBALF or LL-37, (iii) a caf pla mutant was as susceptible to the effect of rBALF or LL-37 as KIM6 was (caf ؉ pla ؉ ), and (iv) only the single caf mutant (pla ؉ ), but not KIM6 or the caf pla double mutant, degraded LL-37. The activity of Pla toward LL-37 was confirmed with pla mutants carrying a single-residue substitution affecting plasminogen cleavage. Taken together, our data indicated that Pla might act as a virulence factor not only by processing plasminogen but also by inactivating CAMPs, particularly when F1 is not expressed.

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“…Developmental and Comparative Immunology j o u r n a l h o m e p a g e : w w w. e l s e v i e r. c o m / l o c a t e / d c i (Adhya et al, 2012;Bulet and Stocklin, 2005;Gueguen et al, 2006;Yang et al, 2000).…”

Section: Contents Lists Available At Sciencedirectmentioning

confidence: 99%

A defensin from clam Venerupis philippinarum: Molecular characterization, localization, antibacterial activity, and mechanism of action

Zhang

Yang

Wang

et al. 2015

Developmental & Comparative Immunology

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A B S T R A C TAntimicrobial peptides (AMPs) are important mediators of the primary host defense system against microbial invasion. In the present study, we cloned and characterized a member of the invertebrate defensin from the clam Venerupis philippinarum, designated VpDef. Amino acid sequence analysis showed that VpDef was similar to defensins from marine mollusks and ticks. In non-stimulated clams, RT-PCR and immunohistochemical analysis revealed that both VpDef mRNA and the encoding peptide were constitutively expressed in hemocytes and mantles, as well as in other major tissues. VpDef transcripts were significantly induced in hemocytes at different time intervals post Vibrio anguillarum infection. The recombinant VpDef (rVpDef) showed the highest activity against Gram-positive bacteria Micrococcus luteus and less effective to Gram-negative bacteria. In addition, incubation of rVpDef with M. luteus at 1 × and 3 × MIC could induce an obvious decrease of the membrane potential and notable changes of membrane permeability in a dose-dependent manner. Membrane integrity and bacterial viability analysis also revealed that rVpDef increased the membrane permeability of M. luteus and then resulted in cell death at 2 × and 10 × MIC. Overall, these results suggest that VpDef has an important function in host defense against invasive pathogens, probably killing microbes by inducing membrane lesions.

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Insect Antimicrobial Peptides: Structures, Properties and Gene Regulation

Cited by 418 publications

References 46 publications

Peptides as toxins/defensins

Peptides as toxins/defensins

Capsular Antigen Fraction 1 and Pla Modulate the Susceptibility of Yersinia pestis to Pulmonary Antimicrobial Peptides Such as Cathelicidin

A defensin from clam Venerupis philippinarum: Molecular characterization, localization, antibacterial activity, and mechanism of action

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