{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T18:06:30Z","timestamp":1790359590237,"version":"4.1.0"},"reference-count":47,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2008,2,22]],"date-time":"2008-02-22T00:00:00Z","timestamp":1203638400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[2008,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Metalloproteinases are abundant enzymes in crotalidae and viperidae snake venoms. Snake venom metalloproteinases (SVMPs) comprise a family of zinc\u2010dependent enzymes, which display many different biological activities. A 23.1 kDa protein was isolated from <jats:italic>Agkistrodon halys<\/jats:italic> (pallas, Chinese viper) snake venom. The toxin is a single chain polypeptide with a molecular weight of 23146.61 and an N\u2010terminal sequence (MIQVLLVTICLAVFPYQGSSIILES) relatively similar to that of other metalloprotein\u2010like proteases isolated from the snake venoms of the <jats:italic>Viperidae<\/jats:italic> family. The antibacterial effect of <jats:italic>Agkistrodon halys<\/jats:italic> metalloproteinase (AHM) on <jats:italic>Burkholderia pseudomallei<\/jats:italic> (strains TES and KHW), <jats:italic>Escherichia coli<\/jats:italic>, <jats:italic>Enterobacter aerogenes<\/jats:italic>, <jats:italic>Proteus vulgaris<\/jats:italic>, <jats:italic>Proteus mirabilis<\/jats:italic>, <jats:italic>Pseudomonas aeruginosa<\/jats:italic> (Gram\u2010negative bacteria) and <jats:italic>Staphylococcus aureus<\/jats:italic> (Gram\u2010positive bacterium) was studied at a concentration 120 \u00b5M. Interestingly, we found that the metalloproteinase exhibited antibacterial properties and was more active against <jats:italic>S. aureus<\/jats:italic>, <jats:italic>P. vulgaris<\/jats:italic>, <jats:italic>P. mirabilis<\/jats:italic> and multi\u2010drug resistant <jats:italic>B. pseudomallei<\/jats:italic> (strain KHW) bacteria. AHM variants with high bacteriostatic activity (MIC 1.875\u201360 \u00b5M) also tended to be less cytotoxic against U\u2010937 human monocytic cells up to 1 mM concentrations. These results suggest that this metalloprotein exerts its antimicrobial effect by altering membrane packing and inhibiting mechanosensitive targets. J. Cell. Physiol. 216: 54\u201368, 2008. \u00a9 2008 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/jcp.21373","type":"journal-article","created":{"date-parts":[[2008,2,22]],"date-time":"2008-02-22T16:16:51Z","timestamp":1203697011000},"page":"54-68","source":"Crossref","is-referenced-by-count":28,"title":["Viper metalloproteinase (<i>Agkistrodon halys<\/i> pallas) with antimicrobial activity against multi\u2010drug resistant human pathogens"],"prefix":"10.1002","volume":"216","author":[{"given":"Ramar Perumal","family":"Samy","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ponnampalam","family":"Gopalakrishnakone","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincent T.K.","family":"Chow","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bow","family":"Ho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,2,22]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1093\/ajcp\/45.4_ts.493"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1021\/jm00061a011"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0163-7258(94)90049-3"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(93)80312-I"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro1098"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi960835f"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(94)36030-8"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/0167-4838(90)90004-Y"},{"key":"e_1_2_6_11_1","first-page":"151","volume-title":"Enzymes from snake venom","author":"Fox JW","year":"1998"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxicon.2005.02.012"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1067\/mai.2002.129801"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1038\/nri1180"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.62.4.1371-1414.1998"},{"key":"e_1_2_6_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(92)90659-S"},{"key":"e_1_2_6_17_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.97.16.8856"},{"key":"e_1_2_6_18_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-2911(08)60145-9"},{"key":"e_1_2_6_19_1","doi-asserted-by":"publisher","DOI":"10.1006\/abbi.1994.1026"},{"key":"e_1_2_6_20_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560030615"},{"key":"e_1_2_6_21_1","doi-asserted-by":"publisher","DOI":"10.1590\/S0100-879X1998000700001"},{"key":"e_1_2_6_22_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M109699200"},{"key":"e_1_2_6_23_1","first-page":"497","article-title":"Thrombocidins, microbicidal proteins from human blood platelets, are C\u2010terminal deletion products of CXC\u2010chemokines","volume":"226","author":"Krijgsveld J","year":"2000","journal-title":"J Biol Chem"},{"key":"e_1_2_6_24_1","doi-asserted-by":"publisher","DOI":"10.1038\/227680a0"},{"key":"e_1_2_6_25_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0041-0101(99)00102-6"},{"key":"e_1_2_6_26_1","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.2000.3724"},{"key":"e_1_2_6_27_1","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(82)90098-8"},{"key":"e_1_2_6_28_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0304-4157(98)00014-8"},{"key":"e_1_2_6_29_1","doi-asserted-by":"publisher","DOI":"10.1016\/0041-0101(82)90016-2"},{"key":"e_1_2_6_30_1","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1042\/bj3420215","article-title":"Lipid\u2010binding and antimicrobial properties of synthetic peptides of bovine apolipoprotein A\u2010II","volume":"342","author":"Motizuki M","year":"1999","journal-title":"Biochem J"},{"key":"e_1_2_6_31_1","unstructured":"National Committee for Clinical Laboratory Standards.1997a.Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria that Grow Aerobically. Approved Standard M7\u2010A4. National Committee for Clinical Standards Wayne Pennsylvania January 1997."},{"key":"e_1_2_6_32_1","unstructured":"National Committee for Clinical Laboratory Standards.1997bPerformance Standards for Antimicrobial Disk Susceptibility Tests: Approved Standard M2\u2010A6. National Committee for Clinical Standards Wayne Pennsylvania January 1997."},{"key":"e_1_2_6_33_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0041-0101(01)00141-6"},{"key":"e_1_2_6_34_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxicon.2005.08.017"},{"key":"e_1_2_6_35_1","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1998.8159"},{"key":"e_1_2_6_36_1","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1055\/s-0037-1614965","article-title":"Thrombin\u2010like enzymes from snake venoms: An updated inventory","volume":"79","author":"Pirkle H","year":"1998","journal-title":"Thromb Haemost"},{"key":"e_1_2_6_37_1","first-page":"287","volume-title":"Pharmaceutical biotechnology","author":"Pretzer D","year":"1993"},{"key":"e_1_2_6_38_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560010505"},{"key":"e_1_2_6_39_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxicon.2006.06.001"},{"key":"e_1_2_6_40_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bmc.2004.03.024"},{"key":"e_1_2_6_41_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxicon.2005.03.008"},{"key":"e_1_2_6_42_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxicon.2006.01.006"},{"key":"e_1_2_6_43_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-291X(02)03001-2"},{"key":"e_1_2_6_44_1","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/dkl093"},{"key":"e_1_2_6_45_1","doi-asserted-by":"publisher","DOI":"10.1093\/jb\/mvg202"},{"key":"e_1_2_6_46_1","doi-asserted-by":"publisher","DOI":"10.1038\/415389a"},{"key":"e_1_2_6_47_1","first-page":"221","article-title":"Characterization of a thrombin\u2010like serine protease, kangshuanmei, isolated from the venom of a Chinese snake, Agkistrodon halys brevicaudus stejnerger","volume":"10","author":"Zhang S","year":"2001","journal-title":"J Nat Toxins"},{"key":"e_1_2_6_48_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0041-0101(99)00193-2"}],"container-title":["Journal of Cellular Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fjcp.21373","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/jcp.21373","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,9]],"date-time":"2023-10-09T23:20:08Z","timestamp":1696893608000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/jcp.21373"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2008,2,22]]},"references-count":47,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2008,7]]}},"alternative-id":["10.1002\/jcp.21373"],"URL":"https:\/\/doi.org\/10.1002\/jcp.21373","archive":["Portico"],"relation":{},"ISSN":["0021-9541","1097-4652"],"issn-type":[{"value":"0021-9541","type":"print"},{"value":"1097-4652","type":"electronic"}],"subject":[],"published":{"date-parts":[[2008,2,22]]}}}