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Salmonella enterica serovar Typhimurium is able to resist antimicrobial peptide killing by induction of the PhoP-PhoQ and PmrA-PmrB two-component systems and the lipopolysaccharide (LPS) modifications they mediate. Murine cathelin-related antimicrobial peptide (CRAMP) has been reported to inhibitS . Typhimurium growthin vitro andin vivo . We hypothesize that infection of human monocyte-derived macrophages (MDMs) withSalmonella enterica serovar Typhi andS . Typhimurium will induce human cathelicidin antimicrobial peptide (CAMP) production, and exposure to LL-37 (processed, active form of CAMP/hCAP18) will lead to upregulation of PmrAB-mediated LPS modifications and increased survivalin vivo . Unlike in mouse macrophages, in which CRAMP is upregulated during infection,camp gene expression was not induced in human MDMs infected withS . Typhi orS . Typhimurium. Upon infection, intracellular levels of ΔphoPQ , ΔpmrAB , and PhoPc S . Typhi decreased over time but were not further inhibited by the vitamin D3 -induced increase incamp expression. MDMs infected with wild-type (WT)S . Typhi orS . Typhimurium released similar levels of proinflammatory cytokines; however, the LPS modification mutant strains dramatically differed in MDM-elicited cytokine levels. Overall, these findings indicate thatcamp is not induced duringSalmonella infection of MDMs nor is key toSalmonella intracellular clearance. However, the cytokine responses from MDMs infected with WT or LPS modification mutant strains differ significantly, indicating a role for LPS modifications in altering the host inflammatory response. Our findings also suggest thatS . Typhi andS . Typhimurium elicit different proinflammatory responses from MDMs, despite being capable of adding similar modifications to their LPS structures.

infection and immunity

Cathelicidin Antimicrobial Peptide Expression Is Not Induced or Required for Bacterial Clearance during Salmonella enterica Infection of Human Monocyte-Derived Macrophages