The SapA Protein Is Involved in Resistance to Antimicrobial Peptide PR-39 and Virulence of Actinobacillus pleuropneumoniae
文献类型: 外文期刊
第一作者: Xie, Fang
作者: Xie, Fang;Wang, Yalei;Li, Gang;Liu, Shuanghong;Cui, Ning;Liu, Siguo;Wang, Chunlai;Wang, Yalei;Langford, Paul R.
作者机构:
关键词: Actinobacillus pleuropneumoniae;SapA;antimicrobial peptide resistance;PR-39;Virulence
期刊名称:FRONTIERS IN MICROBIOLOGY ( 影响因子:5.64; 五年影响因子:6.32 )
ISSN: 1664-302X
年卷期: 2017 年 8 卷
页码:
收录情况: SCI
摘要: Antimicrobial peptides are essential to the innate immune defense of the mammal against bacterial infection. However, pathogenic bacteria have evolved multiple strategies to resist and evade antimicrobial peptides, which is vital to bacterial survival and colonization in hosts. PR-39 is a linear porcine antimicrobial peptide containing 39 amino acid residues with a high proline content. Resistance to antimicrobial peptide PR-39 has been observed in Actinobacillus pleuropneumoniae. However, little is known about the factors required for this resistance. In the present study, PR-39 exposure increased the expression of the sapA gene in A. pleuropneumoniae. The sapA gene, which encodes a putative peptide transport periplasmic protein, was deleted from this bacterium. The Delta sapA mutant showed increased sensitivity to PR-39 compared to the wild-type MD12 and complemented P Delta sapA strains. However, the Delta sapA mutant did not exhibit any alterations in outer membrane integrity. Scanning electron microscopy showed that the Delta sapA mutant displayed morphological defects, as indicated by a deformed and sunken shape after PR-39 treatment. In addition, disruption of the SapA protein led to reduced colonization and attenuated virulence of A. pleuropneumoniae in the BALB/c mouse model. Collectively, these data suggest that SapA acts as one mechanism for A. pleuropneumoniae to counteract PR-39-mediated killing. To the best of our knowledge, this is the first study to show a mechanism underlying antimicrobial peptide resistance in A. pleuropneumoniae.
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