2. Academic Validation
  3. AP-57/C10orf99 is a new type of multifunctional antimicrobial peptide

AP-57/C10orf99 is a new type of multifunctional antimicrobial peptide

  • Biochem Biophys Res Commun. 2015 Feb 13;457(3):347-52. doi: 10.1016/j.bbrc.2014.12.115.
Meijia Yang 1,  Mei Tang 1,  Xianjun Ma 1,  Lijia Yang 1,  Jiangpeng He 1,  Xirui Peng 1,  Gang Guo 1,  Liangxue Zhou 2,  Na Luo 3,  Zhu Yuan 4,  Aiping Tong 5
Affiliations

Affiliations

  • 1 The State Key Laboratory of Biotherapy and Cancer Center/Collaborative Innovation Center of Biotherapy, West China Hospital, West China Medical School, Sichuan University, Chengdu 610041, China.
  • 2 Department of Neurosurgery, West China Hospital, West China Medical School, Sichuan University, Chengdu 610041, China.
  • 3 Nankai University School of Medicine/Collaborative Innovation Center of Biotherapy, Tianjin 300071, China.
  • 4 The State Key Laboratory of Biotherapy and Cancer Center/Collaborative Innovation Center of Biotherapy, West China Hospital, West China Medical School, Sichuan University, Chengdu 610041, China. Electronic address: yuanzhu@scu.edu.cn.
  • 5 The State Key Laboratory of Biotherapy and Cancer Center/Collaborative Innovation Center of Biotherapy, West China Hospital, West China Medical School, Sichuan University, Chengdu 610041, China. Electronic address: aipingtong@scu.edu.cn.
PMID: 25585381 DOI: 10.1016/j.bbrc.2014.12.115
Abstract

Antimicrobial Peptides (AMPs) are an evolutionarily conserved component of the innate immune response that provides host defence at skin and mucosal surfaces. Here, we report the identification and characterization of a new type human AMPs, termed AP-57 (Antimicrobial Peptide with 57 amino acid residues), which is also known as C10orf99 (chromosome 10 open reading frame 99). AP-57 is a short basic amphiphilic peptide with four cysteines and a net charge +14 (MW = 6.52, PI = 11.28). The highest expression of AP-57 were detected in the mucosa of stomach and colon through immunohistochemical assay. Epithelium of skin and esophagus show obvious positive staining and strong positive staining were also observed in some tumor and/or their adjacent tissues, such as esophagus Cancer, hepatocellular carcinoma, squamous cell carcinoma and invasive ductal carcinoma. AP-57 exhibited broad-spectrum antimicrobial activities against Gram-positive Staphylococcus aureus, Actinomyce, and Fungi Aspergillus niger as well as mycoplasma and lentivirus. AP-57 also exhibited DNA binding capacity and specific cytotoxic effects against human B-cell lymphoma Raji. Compared with other human AMPs, AP-57 has its distinct characteristics, including longer sequence length, four cysteines, highly cationic character, cell-specific toxicity, DNA binding and tissue-specific expressing patterns. Together, AP-57 is a new type of multifunctional AMPs worthy further investigation.

Keywords

AMPs; Antibacterial peptide; Antimicrobial Peptide-57; Antimicrobial proteins; C10orf99; Defensins.

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