Edgar Neri-Castro , Vanessa Zarzosa , Bruno Lomonte , Fernando Zamudio , Lorena Hernandez-Orihuela , Alejandro Olvera-Rodríguez , Audrey Michelle Rodríguez-Solís , Miguel Borja , Uri O. García-Vázquez , Jason M. Jones , Chistopher L. Parkinson , Alejandro Alagón
{"title":"Exploring Venom Diversity in Mixcoatlus browni and Mixcoatlus barbouri:两种含有类似克罗毒素的墨西哥稀有蛇类的比较分析。","authors":"Edgar Neri-Castro , Vanessa Zarzosa , Bruno Lomonte , Fernando Zamudio , Lorena Hernandez-Orihuela , Alejandro Olvera-Rodríguez , Audrey Michelle Rodríguez-Solís , Miguel Borja , Uri O. García-Vázquez , Jason M. Jones , Chistopher L. Parkinson , Alejandro Alagón","doi":"10.1016/j.biochi.2024.05.015","DOIUrl":null,"url":null,"abstract":"<div><p>The genus <em>Mixcoatlus</em> is composed of three species: <em>Mixcoatlus barbouri</em>, <em>M. browni</em>, and <em>M. melanurus</em>, of which the venom composition of <em>M. melanurus</em>, the most common species of the three, has only recently been described. However, very little is known about the natural history of <em>M. barbouri</em> and <em>M. browni</em>, and the venom composition of these two species has remained thus far unexplored. In this study we characterize the proteomic profiles and the main biochemical and toxic activities of these two venoms. Proteomic data obtained by shotgun analysis of whole venom identified 12 protein families for <em>M. barbouri</em>, and 13 for <em>M</em>. <em>browni</em>. The latter venom was further characterized by using a quantitative ‘venomics’ protocol, which revealed that it is mainly composed of 51.1 % phospholipases A<sub>2</sub> (PLA<sub>2</sub>), 25.5 % snake venom serine proteases (SVSP), 4.6 % <span>l</span>-amino oxidases (LAO), and 3.6 % snake venom metalloproteases (SVMP), with lower percentages other six protein families. Both venoms contained homologs of the basic and acidic subunits of crotoxin. However, due to limitations in <em>M. barbouri</em> venom availability, we could only characterize the crotoxin-like protein of <em>M. browni</em> venom, which we have named Mixcoatlutoxin. It exhibited a lethal potency in mice like that described for classical rattlesnake crotoxins. These findings expand knowledge on the distribution of crotoxin-like heterodimeric proteins in viper snake species. Further investigation of the bioactivities of the venom of <em>M. barbouri</em>, on the other hand, remains necessary.</p></div>","PeriodicalId":251,"journal":{"name":"Biochimie","volume":"225 ","pages":"Pages 81-88"},"PeriodicalIF":3.3000,"publicationDate":"2024-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Exploring venom diversity in Mixcoatlus browni and Mixcoatlus barbouri: A comparative analysis of two rare Mexican snake species with crotoxin-like presence\",\"authors\":\"Edgar Neri-Castro , Vanessa Zarzosa , Bruno Lomonte , Fernando Zamudio , Lorena Hernandez-Orihuela , Alejandro Olvera-Rodríguez , Audrey Michelle Rodríguez-Solís , Miguel Borja , Uri O. García-Vázquez , Jason M. Jones , Chistopher L. Parkinson , Alejandro Alagón\",\"doi\":\"10.1016/j.biochi.2024.05.015\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The genus <em>Mixcoatlus</em> is composed of three species: <em>Mixcoatlus barbouri</em>, <em>M. browni</em>, and <em>M. melanurus</em>, of which the venom composition of <em>M. melanurus</em>, the most common species of the three, has only recently been described. However, very little is known about the natural history of <em>M. barbouri</em> and <em>M. browni</em>, and the venom composition of these two species has remained thus far unexplored. In this study we characterize the proteomic profiles and the main biochemical and toxic activities of these two venoms. Proteomic data obtained by shotgun analysis of whole venom identified 12 protein families for <em>M. barbouri</em>, and 13 for <em>M</em>. <em>browni</em>. The latter venom was further characterized by using a quantitative ‘venomics’ protocol, which revealed that it is mainly composed of 51.1 % phospholipases A<sub>2</sub> (PLA<sub>2</sub>), 25.5 % snake venom serine proteases (SVSP), 4.6 % <span>l</span>-amino oxidases (LAO), and 3.6 % snake venom metalloproteases (SVMP), with lower percentages other six protein families. Both venoms contained homologs of the basic and acidic subunits of crotoxin. However, due to limitations in <em>M. barbouri</em> venom availability, we could only characterize the crotoxin-like protein of <em>M. browni</em> venom, which we have named Mixcoatlutoxin. It exhibited a lethal potency in mice like that described for classical rattlesnake crotoxins. These findings expand knowledge on the distribution of crotoxin-like heterodimeric proteins in viper snake species. Further investigation of the bioactivities of the venom of <em>M. barbouri</em>, on the other hand, remains necessary.</p></div>\",\"PeriodicalId\":251,\"journal\":{\"name\":\"Biochimie\",\"volume\":\"225 \",\"pages\":\"Pages 81-88\"},\"PeriodicalIF\":3.3000,\"publicationDate\":\"2024-05-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimie\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0300908424001172\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimie","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0300908424001172","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Exploring venom diversity in Mixcoatlus browni and Mixcoatlus barbouri: A comparative analysis of two rare Mexican snake species with crotoxin-like presence
The genus Mixcoatlus is composed of three species: Mixcoatlus barbouri, M. browni, and M. melanurus, of which the venom composition of M. melanurus, the most common species of the three, has only recently been described. However, very little is known about the natural history of M. barbouri and M. browni, and the venom composition of these two species has remained thus far unexplored. In this study we characterize the proteomic profiles and the main biochemical and toxic activities of these two venoms. Proteomic data obtained by shotgun analysis of whole venom identified 12 protein families for M. barbouri, and 13 for M. browni. The latter venom was further characterized by using a quantitative ‘venomics’ protocol, which revealed that it is mainly composed of 51.1 % phospholipases A2 (PLA2), 25.5 % snake venom serine proteases (SVSP), 4.6 % l-amino oxidases (LAO), and 3.6 % snake venom metalloproteases (SVMP), with lower percentages other six protein families. Both venoms contained homologs of the basic and acidic subunits of crotoxin. However, due to limitations in M. barbouri venom availability, we could only characterize the crotoxin-like protein of M. browni venom, which we have named Mixcoatlutoxin. It exhibited a lethal potency in mice like that described for classical rattlesnake crotoxins. These findings expand knowledge on the distribution of crotoxin-like heterodimeric proteins in viper snake species. Further investigation of the bioactivities of the venom of M. barbouri, on the other hand, remains necessary.
期刊介绍:
Biochimie publishes original research articles, short communications, review articles, graphical reviews, mini-reviews, and hypotheses in the broad areas of biology, including biochemistry, enzymology, molecular and cell biology, metabolic regulation, genetics, immunology, microbiology, structural biology, genomics, proteomics, and molecular mechanisms of disease. Biochimie publishes exclusively in English.
Articles are subject to peer review, and must satisfy the requirements of originality, high scientific integrity and general interest to a broad range of readers. Submissions that are judged to be of sound scientific and technical quality but do not fully satisfy the requirements for publication in Biochimie may benefit from a transfer service to a more suitable journal within the same subject area.