title: Antibacterial properties of Acinetobacter baumannii phage Abp1 endolysin (PlyAB1).
abstract: BACKGROUND
  Acinetobacter baumannii has emerged as one of the most important hospital-acquired pathogens in the world, because of its resistance to almost all available antibiotic drugs. Endolysins from phages are attracting increasing interest as potential antimicrobial agents, especially for drug-resistant bacteria. We previously isolated and characterized Abp1, a virulent phage targeting the multidrug-resistant A. baumannii strain, AB1.
  
  
  METHODS
  To evaluate the antimicrobial potential of endolysin from the Abp1 phage, the endolysin gene plyAB1 was cloned and over-expressed in Escherichia coli, and the lytic activity of the recombinant protein (PlyAB1) was tested by turbidity assessment and bacteria counting assays.
  
  
  RESULTS
  PlyAB1 exhibits a marked lytic activity against A. baumannii AB1, as shown by a decrease in the number of live bacteria following treatment with the enzyme. Moreover, PlyAB1 displayed a highly specific lytic effect against all of the 48 hospital-derived pandrug-resistant A. baumannii isolates that were tested. These isolates were shown to belong to different ST clones by multilocus sequence typing.
  
  
  CONCLUSIONS
  The results presented here show that PlyAB1 has potential as an antibiotic against drug-resistant A. baumannii.
authors.affiliation: State Key Laboratory of Trauma, Burns and Combined Injury, Institute of Burn Research, Southwest Hospital, Third Military Medical University, Chongqing, China. haitao3140@sina.com.|Department of Microbiology, Third Military Medical University, Chongqing, China. haitao3140@sina.com.
authors.forename: Guangtao
authors.initials: G
authors.lastname: Huang
authors.affiliation: Department of Biochemistry and Molecular Biology, Third Military Medical University, Chongqing, China. shenxiaodong77@aliyun.com.
authors.forename: Xiaodong
authors.initials: X
authors.lastname: Shen
authors.affiliation: State Key Laboratory of Trauma, Burns and Combined Injury, Institute of Burn Research, Southwest Hospital, Third Military Medical University, Chongqing, China. 346076091@qq.com.
authors.forename: Yali
authors.initials: Y
authors.lastname: Gong
authors.affiliation: State Key Laboratory of Trauma, Burns and Combined Injury, Institute of Burn Research, Southwest Hospital, Third Military Medical University, Chongqing, China. 598852689@qq.com.
authors.forename: Zhiwei
authors.initials: Z
authors.lastname: Dong
authors.affiliation: Department of Microbiology, Third Military Medical University, Chongqing, China. 182484366@qq.com.
authors.forename: Xia
authors.initials: X
authors.lastname: Zhao
authors.affiliation: Department of Microbiology, Third Military Medical University, Chongqing, China. 84686485@qq.com.
authors.forename: Wei
authors.initials: W
authors.lastname: Shen
authors.affiliation: Department of Microbiology, Third Military Medical University, Chongqing, China. 190096912@qq.com.
authors.forename: Jing
authors.initials: J
authors.lastname: Wang
authors.affiliation: Department of Microbiology, Third Military Medical University, Chongqing, China. hufuquan2009@aliyun.com.
authors.forename: Fuquan
authors.initials: F
authors.lastname: Hu
authors.affiliation: State Key Laboratory of Trauma, Burns and Combined Injury, Institute of Burn Research, Southwest Hospital, Third Military Medical University, Chongqing, China. yizhipen@sina.com.
authors.forename: Yizhi
authors.initials: Y
authors.lastname: Peng
mesh_terms: D040981:Acinetobacter baumannii / Q000187:drug effects* / Q000821:virology; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001435:Bacteriophages / Q000201:enzymology*; D024881:Drug Resistance, Bacterial; D010450:Endopeptidases / Q000494:pharmacology*; D011994:Recombinant Proteins / Q000494:pharmacology; D014764:Viral Proteins / Q000494:pharmacology*
chemical_list: D000900:Anti-Bacterial Agents; D011994:Recombinant Proteins; D014764:Viral Proteins; D010450:Endopeptidases; C001143:endolysin; C000602256:endolysin, Acinetobacter baumannii phage