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A bovine myeloid antimicrobial peptide (BMAP-28) and its analogs kill pan-drug-resistant Acinetobacter baumannii by

Yijie Guo1,2, Meng Xun1,2, Jing Han1,3

  • 1Key Laboratory of Environment and Genes Related to Diseases, Xi'an Jiaotong University, Ministry of Education of China.

Medicine
|October 19, 2018
PubMed

Insights

Bovine myeloid antimicrobial peptide (BMAP-28) and its analogs effectively inhibit pan-drug-resistant Acinetobacter baumannii (PDRAB). BMAP-28 shows potent antimicrobial activity and potential mechanisms involving outer membrane protein A interaction.

Area of Science:

  • Microbiology
  • Biochemistry
  • Drug Discovery

Background:

  • Antimicrobial peptides (AMPs) are crucial in combating microbial infections.
  • Pan-drug-resistant Acinetobacter baumannii (PDRAB) poses a significant global health threat.
  • Cathelicidin-derived peptides, like BMAP-28, are investigated for their antimicrobial potential.

Purpose of the Study:

  • To evaluate the antimicrobial activity of BMAP-28 and its analogs against PDRAB.
  • To elucidate the mechanism of action of BMAP-28 against PDRAB.

Main Methods:

  • Minimal inhibitory concentration (MIC) analysis and short-time killing assays.
  • Field emission scanning electron microscopy (FE-SEM) for cell surface analysis.
  • Quartz crystal microbalance (QCM) to study peptide-protein interactions.

Main Results:

  • BMAP-28 and its analogs demonstrated significant inhibitory effects and rapid killing of PDRAB.
  • BMAP-28 exhibited superior activity compared to its analogs, causing visible cell surface damage.
  • QCM analysis indicated a potential interaction between BMAP-28 and Acinetobacter baumannii outer membrane protein A (AbOmpA).

Conclusions:

  • BMAP-28 is a promising candidate for treating PDRAB infections.
  • The antimicrobial efficacy of BMAP-28 is linked to its interaction with AbOmpA.

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