{"title":"d-aspartate, an amino-acid important for human health, supports anaerobic respiration in several Campylobacter species","authors":"","doi":"10.1016/j.resmic.2024.104219","DOIUrl":null,"url":null,"abstract":"<div><p>Despite being classified as microaerophilic microorganisms, most <span><span>Campylobacter</span></span> species can grow anaerobically, using formate or molecular hydrogen (H<sub>2</sub>) as electron donors, and various nitrogenous and sulfurous compounds as electron acceptors. Herein, we showed that both <span>l</span>-asparagine (<span>l</span>-Asn) and <span>l</span>-aspartic acid (<span>l</span>-Asp) bolster H<sub>2</sub><span>-driven anaerobic growth in several </span><span><em>Campylobacter</em></span> species, whereas the <span>d-</span><span><span>enantiomer form of both </span>asparagine (</span><span>d</span><span>-Asn) and aspartic acid (</span><span>d</span>-Asp) only increased anaerobic growth in <span><span>Campylobacter concisus</span></span> strain 13826 and <span><em>Campylobacter ureolyticus</em></span> strain NCTC10941. A gene annotated as <em>racD</em> encoding for a putative <span>d</span>/<span>l</span><span>-Asp racemase was identified in the genome of both strains. Disruption of </span><em>racD</em> in <em>Cc</em>13826 resulted in the inability of the mutant strain to use either <span>d-</span>enantiomer during anaerobic growth. Hence, our results suggest that the <em>racD</em> gene is required for campylobacters to use either <span>d</span>-Asp or <span>d</span>-Asn. The use of <span>d</span>-Asp by various human opportunistic bacterial pathogens, including <em>C. concisus</em>, <em>C. ureolyticus</em>, and also possibly select strains of <em>Campylobacter gracilis</em>, <span><span>Campylobacter rectus</span></span> and <em>Campylobacter showae</em>, is significant, because <span>d</span><span>-Asp is an important signal molecule for both human nervous and neuroendocrine systems. To our knowledge, this is the first report of pathogens scavenging a </span><span>d-</span><span>amino acid essential for human health.</span></p></div>","PeriodicalId":2,"journal":{"name":"ACS Applied Bio Materials","volume":null,"pages":null},"PeriodicalIF":4.6000,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS Applied Bio Materials","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0923250824000561","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"MATERIALS SCIENCE, BIOMATERIALS","Score":null,"Total":0}
引用次数: 0
Abstract
Despite being classified as microaerophilic microorganisms, most Campylobacter species can grow anaerobically, using formate or molecular hydrogen (H2) as electron donors, and various nitrogenous and sulfurous compounds as electron acceptors. Herein, we showed that both l-asparagine (l-Asn) and l-aspartic acid (l-Asp) bolster H2-driven anaerobic growth in several Campylobacter species, whereas the d-enantiomer form of both asparagine (d-Asn) and aspartic acid (d-Asp) only increased anaerobic growth in Campylobacter concisus strain 13826 and Campylobacter ureolyticus strain NCTC10941. A gene annotated as racD encoding for a putative d/l-Asp racemase was identified in the genome of both strains. Disruption of racD in Cc13826 resulted in the inability of the mutant strain to use either d-enantiomer during anaerobic growth. Hence, our results suggest that the racD gene is required for campylobacters to use either d-Asp or d-Asn. The use of d-Asp by various human opportunistic bacterial pathogens, including C. concisus, C. ureolyticus, and also possibly select strains of Campylobacter gracilis, Campylobacter rectus and Campylobacter showae, is significant, because d-Asp is an important signal molecule for both human nervous and neuroendocrine systems. To our knowledge, this is the first report of pathogens scavenging a d-amino acid essential for human health.