{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,6]],"date-time":"2026-05-06T13:14:36Z","timestamp":1778073276717,"version":"3.51.4"},"reference-count":58,"publisher":"Oxford University Press (OUP)","license":[{"start":{"date-parts":[[2026,4,23]],"date-time":"2026-04-23T00:00:00Z","timestamp":1776902400000},"content-version":"vor","delay-in-days":112,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,1,8]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>In many bacterial species, carbonic anhydrases (CAs) have been shown to play crucial roles in metabolism, cellular pH homeostasis, growth, and\/or pathogenicity. Thus, these enzymes are considered as vital targets of drug development. We investigated the importance of CAs to growth, cellular metabolism, pH homeostasis, and intracellular survival of Neisseria gonorrhoeae. BLAST searches of N. gonorrhoeae genome sequence revealed the presence of three genes respectively homologous to \u03b1CA, \u03b2CA, and \u03b3CA genes of other bacteria. The putative \u03b1CA protein of N. gonorrhoeae was found to localize to the periplasm, whereas the other two proteins were predicted to reside in the cytoplasm. All three CAs of N. gonorrhoeae shared up to 99% identity with CAs of other bacteria. Three isogenic mutants were constructed by disrupting the \u03b1CA, \u03b2CA, and \u03b3CA genes. The mutants were complemented by reincorporating the disrupted CA genes into each of the mutants. All three CA mutants were similar to the parent N. gonorrhoeae in terms of their growth at 5% CO2. Nevertheless, unlike the parent or the other CA mutants, the \u0394\u03b2CA mutant failed to grow at ambient air or 2% or 3% CO2, highlighting the importance of the \u03b2CA for CO2 hydration in decreased CO2 environments. The pH of the culture medium decreased during proliferation of N. gonorrhoeae cells, nevertheless, the least decline of pH was observed in the \u0394\u03b2CA mutant culture. These findings suggest that N. gonorrhoeae prefers slightly acidic growth environment and \u03b2CA is important for pH homeostasis. Acetyl-CoA, which is a substrate for Malonyl-CoA biosynthesis in cell, was recovered in relatively increased amounts from the \u0394\u03b1CA and \u0394\u03b2CA mutant cells, underscoring a possible relationship between the \u03b1CA and \u03b2CA functions and cellular metabolism. Relative to the parent strain, the \u0394\u03b1CA and \u0394\u03b2CA mutants were recovered from infected ME-180 cells in decreased numbers, highlighting the importance of the \u03b1CA and \u03b2CA in intracellular survival and replication. Several other publications have reported \u03b1CA as an essential protein for the viability of N. gonorrhoeae. Since our findings on \u03b1CA were not in agreement with those published reports, we constructed an additional mutant of \u03b1CA gene by deleting the entire ORF of this gene. This second \u0394\u03b1CA mutant was similar to our first \u0394\u03b1CA mutant and the parent strain in terms of growth in ambient CO2 concentrations. Thus, we conclude that \u03b1CA is dispensable for the viability of N. gonorrhoeae. Unlike our \u0394\u03b1CA or \u0394\u03b2CA mutants, our \u0394\u03b3CA mutant was not different from the parent in growth, metabolism, or intracellular survival. Overall, we conclude that \u03b1CA is dispensable for the viability, growth, and pH homeostasis but is important for metabolism and intracellular survival of N. gonorrhoeae. The \u03b2CA is indispensable for the viability of N. gonorrhoeae, and also plays important roles in growth, pH homeostasis, metabolism, and intracellular survival. Contrary to the other two CAs, the \u03b3CA does not play detectable roles in growth, metabolism, pH dynamics, or intracellular survival.<\/jats:p>","DOI":"10.1093\/femsmc\/xtag021","type":"journal-article","created":{"date-parts":[[2026,4,23]],"date-time":"2026-04-23T11:40:27Z","timestamp":1776944427000},"source":"Crossref","is-referenced-by-count":0,"title":["Roles of three carbonic anhydrases in\n                    <i>in vitro<\/i>\n                    growth, pH homeostasis, metabolism, and intracellular survival of\n                    <i>Neisseria gonorrhoeae<\/i>"],"prefix":"10.1093","volume":"7","author":[{"given":"Sanjay V","family":"Alokabandara","sequence":"first","affiliation":[{"name":"SAPRA Biomedicals, Corporate Research Center , Blacksburg, VA 24060 ,","place":["United States"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hsin-Wen","family":"Liang","sequence":"additional","affiliation":[{"name":"Virginia Polytechnic Institute and State University Department of Biomedical Sciences and Pathobiology, Virginia-Maryland College of Veterinary Medicine, , Blacksburg, VA 24061 ,","place":["United States"]},{"name":"Northeastern University Department of Biology, , Boston, MA 02115 ,","place":["United States"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2562-1810","authenticated-orcid":false,"given":"Aloka B","family":"Bandara","sequence":"additional","affiliation":[{"name":"SAPRA Biomedicals, Corporate Research Center , Blacksburg, VA 24060 ,","place":["United States"]},{"name":"Virginia Polytechnic Institute and State University Department of Biomedical Sciences and Pathobiology, Virginia-Maryland College of Veterinary Medicine, , Blacksburg, VA 24061 ,","place":["United States"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2026,4,23]]},"reference":[{"key":"2026050608320769200_bib1","doi-asserted-by":"publisher","first-page":"4111","DOI":"10.1128\/IAI.00409-09","article-title":"Bicarbonate Induces Vibrio cholerae virulence gene expression by enhancing ToxT activity","volume":"77","author":"Abuaita","year":"2009","journal-title":"Infect Immun"},{"key":"2026050608320769200_bib2","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1080\/14756366.2021.1991336","article-title":"Repurposing FDA-approved sulphonamide carbonic anhydrase inhibitors for treatment of Neisseria gonorrhoeae","volume":"37","author":"Abutaleb","year":"2022","journal-title":"J Enzyme Inhib Med Chem"},{"key":"2026050608320769200_bib3","doi-asserted-by":"publisher","first-page":"721","DOI":"10.1111\/1462-2920.13092","article-title":"Major contribution of the type II beta carbonic anhydrase CanB (Cj0237) to the capnophilic growth phenotype of Campylobacter jejuni","volume":"18","author":"Al-Haideri","year":"2016","journal-title":"Environ Microbiol"},{"key":"2026050608320769200_bib4","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.01225-19","article-title":"Repurposing salicylamide for combating multidrug-resistant Neisseria gonorrhoeae","volume":"63","author":"Alhashimi","year":"2019","journal-title":"Antimicrob Agents Chemother"},{"key":"2026050608320769200_bib5","doi-asserted-by":"publisher","first-page":"1311","DOI":"10.1093\/infdis\/jiu230","article-title":"A role for lactate dehydrogenases in the survival of Neisseria gonorrhoeae in human polymorphonuclear leukocytes and cervical epithelial cells","volume":"210","author":"Atack","year":"2014","journal-title":"J Infect Dis"},{"key":"2026050608320769200_bib6","doi-asserted-by":"publisher","first-page":"7197","DOI":"10.1128\/jb.179.22.7197-7200.1997","article-title":"Carbonic anhydrase in Acetobacterium woodii and other acetogenic bacteria","volume":"179","author":"Braus-Stromeyer","year":"1997","journal-title":"J Bacteriol"},{"key":"2026050608320769200_bib7","doi-asserted-by":"publisher","first-page":"527","DOI":"10.3109\/14756366.2015.1051042","article-title":"The history and rationale of using carbonic anhydrase inhibitors in the treatment of peptic ulcers. 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