title: N-Terminal Polypeptide of Annexin A2 Decreases Infection of Mycoplasma hyorhinis to Gastric Cancer Cells.
abstract: Mycoplasma infection in human and its contamination in cell cultures are worldwide problems. The drugs currently available for preventing or treating mycoplasma infection suffer from low sensitivity, strong resistance and high toxicity. Our previous work showed that Mycoplasma hyorhinis (M. hyorhinis) infection was mediated by the interaction between p37 of M. hyorhinis and Annexin A2 (ANXA2) of host cells, however the translational value of this mechanism was unknown. Herein, we synthesized the N-terminal of ANXA2 polypeptide (A2PP) and found that A2PP could decrease the infection of M. hyorhinis to gastric cancer cells and block M. hyorhinis infection-induced cell migration. Furthermore, we found that A2PP could reduce M. hyorhinis contamination of passage cells. Moreover, compared with the commercial antibiotics commonly used in cell culture to prevent M. hyorhinis infection, A2PP demonstrated a more effectiveness but a low toxicity on cell growth. Thus, our study for the first time revealed A2PP's potential for the treatment and prevention of M. hyorhinis infection.
authors.affiliation: Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, Peking University Cancer Hospital & Institute, Beijing, China.
authors.forename: Shiqin
authors.initials: S
authors.lastname: Yuan
authors.affiliation: Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, Peking University Cancer Hospital & Institute, Beijing, China.
authors.forename: Like
authors.initials: L
authors.lastname: Qu
authors.affiliation: Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, Peking University Cancer Hospital & Institute, Beijing, China.
authors.forename: Chengchao
authors.initials: C
authors.lastname: Shou
mesh_terms: D051696:Activating Transcription Factors / Q000235:genetics / Q000378:metabolism; D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry / Q000378:metabolism; D017306:Annexin A2 / Q000737:chemistry*; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D022782:CCAAT-Enhancer-Binding Protein-beta / Q000235:genetics / Q000378:metabolism; D045744:Cell Line, Tumor; D002465:Cell Movement / Q000187:drug effects; D049109:Cell Proliferation / Q000187:drug effects; D002470:Cell Survival / Q000187:drug effects; D002939:Ciprofloxacin / Q000494:pharmacology; D018920:Coculture Techniques; D004269:DNA, Bacterial / Q000032:analysis; D006801:Humans; D047468:Immunoprecipitation; D045790:Mycoplasma hyorhinis / Q000187:drug effects / Q000235:genetics / Q000502:physiology*; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism / Q000494:pharmacology; D011485:Protein Binding; D060888:Real-Time Polymerase Chain Reaction; D013274:Stomach Neoplasms / Q000378:metabolism / Q000473:pathology; D051742:Transcription Factor CHOP / Q000235:genetics / Q000378:metabolism
chemical_list: C507532:ATF5 protein, human; D051696:Activating Transcription Factors; D048868:Adaptor Proteins, Signal Transducing; D017306:Annexin A2; D000900:Anti-Bacterial Agents; D022782:CCAAT-Enhancer-Binding Protein-beta; C545012:CEBPB protein, human; C497249:DDIT3 protein, human; D004269:DNA, Bacterial; D010455:Peptides; C553975:p37 protein, human; D051742:Transcription Factor CHOP; D002939:Ciprofloxacin
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