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  • D-alanine modification of a protease-susceptible outer membrane component by the Bordetella pertussis dra locus promotes resistance to antimicrobial peptides and polymorphonuclear leukocyte-mediated killing.

D-alanine modification of a protease-susceptible outer membrane component by the Bordetella pertussis dra locus promotes resistance to antimicrobial peptides and polymorphonuclear leukocyte-mediated killing.

Journal of bacteriology (2013-09-10)
Neetu Kumra Taneja, Tridib Ganguly, Lauren O Bakaletz, Kimberly J Nelson, Purnima Dubey, Leslie B Poole, Rajendar Deora
ABSTRACT

Bordetella pertussis is the causative agent of pertussis, a highly contagious disease of the human respiratory tract. Despite very high vaccine coverage, pertussis has reemerged as a serious threat in the United States and many developing countries. Thus, it is important to pursue research to discover unknown pathogenic mechanisms of B. pertussis. We have investigated a previously uncharacterized locus in B. pertussis, the dra locus, which is homologous to the dlt operons of Gram-positive bacteria. The absence of the dra locus resulted in increased sensitivity to the killing action of antimicrobial peptides (AMPs) and human phagocytes. Compared to the wild-type cells, the mutant cells bound higher levels of cationic proteins and peptides, suggesting that dra contributes to AMP resistance by decreasing the electronegativity of the cell surface. The presence of dra led to the incorporation of d-alanine into an outer membrane component that is susceptible to proteinase K cleavage. We conclude that dra encodes a virulence-associated determinant and contributes to the immune resistance of B. pertussis. With these findings, we have identified a new mechanism of surface modification in B. pertussis which may also be relevant in other Gram-negative pathogens.

MATERIALS
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Product Description

Sigma-Aldrich
Proteinase K from Tritirachium album, buffered aqueous glycerol solution, for molecular biology, ≥800 units/mL
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Sigma-Aldrich
Proteinase K from Tritirachium album, ≥500 units/mL, buffered aqueous glycerol solution
Product P5568 is not currently sold in your country. Contact Technical Service
Sigma-Aldrich
Proteinase K from Tritirachium album, lyophilized powder, ≥30 units/mg protein
Pricing and availability is not currently available.
Sigma-Aldrich
Proteinase K from Tritirachium album, ≥3.0 unit/mg solid, lyophilized powder
Pricing and availability is not currently available.
Sigma-Aldrich
Proteinase K from Tritirachium album, lyophilized powder, BioUltra, ≥30 units/mg protein, for molecular biology
Pricing and availability is not currently available.
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Proteinase K from Tritirachium album, Reagents designed and manufactured under current ISO 13485 certification.
Pricing and availability is not currently available.