{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T09:43:56Z","timestamp":1790502236526,"version":"4.1.0"},"reference-count":70,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2017,6,15]],"date-time":"2017-06-15T00:00:00Z","timestamp":1497484800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["AI073994"],"award-info":[{"award-number":["AI073994"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2017,6,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Although mycoplasmas have small genomes, many of them, including the HIV-associated opportunist\n            <jats:named-content content-type=\"genus-species\">Mycoplasma penetrans<\/jats:named-content>\n            , construct a polar attachment organelle (AO) that is used for both adherence to host cells and gliding motility. However, the irregular phylogenetic distribution of similar structures within the mycoplasmas, as well as compositional and ultrastructural differences among these AOs, suggests that AOs have arisen several times through convergent evolution. We investigated the ultrastructure and protein composition of the cytoskeleton-like material of the\n            <jats:named-content content-type=\"genus-species\">M. penetrans<\/jats:named-content>\n            AO with several forms of microscopy and biochemical analysis, to determine whether the\n            <jats:named-content content-type=\"genus-species\">M. penetrans<\/jats:named-content>\n            AO was constructed at the molecular level on principles similar to those of other mycoplasmas, such as\n            <jats:named-content content-type=\"genus-species\">Mycoplasma pneumoniae<\/jats:named-content>\n            and\n            <jats:named-content content-type=\"genus-species\">Mycoplasma mobile<\/jats:named-content>\n            . We found that the\n            <jats:named-content content-type=\"genus-species\">M. penetrans<\/jats:named-content>\n            AO interior was generally dissimilar from that of other mycoplasmas, in that it exhibited considerable heterogeneity in size and shape, suggesting a gel-like nature. In contrast, several of the 12 potential protein components identified by mass spectrometry of\n            <jats:named-content content-type=\"genus-species\">M. penetrans<\/jats:named-content>\n            detergent-insoluble proteins shared certain distinctive biochemical characteristics with\n            <jats:named-content content-type=\"genus-species\">M. pneumoniae<\/jats:named-content>\n            AO proteins, although not with\n            <jats:named-content content-type=\"genus-species\">M. mobile<\/jats:named-content>\n            proteins. We conclude that convergence between\n            <jats:named-content content-type=\"genus-species\">M. penetrans<\/jats:named-content>\n            and\n            <jats:named-content content-type=\"genus-species\">M. pneumoniae<\/jats:named-content>\n            AOs extends to the molecular level, leading to the possibility that the less organized material in both\n            <jats:named-content content-type=\"genus-species\">M. pneumoniae<\/jats:named-content>\n            and\n            <jats:named-content content-type=\"genus-species\">M. penetrans<\/jats:named-content>\n            is the substance principally responsible for the organization and function of the AO.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            <jats:named-content content-type=\"genus-species\">Mycoplasma penetrans<\/jats:named-content>\n            is a bacterium that infects HIV-positive patients and may contribute to the progression of AIDS. It attaches to host cells through a structure called an AO, but it is not clear how it builds this structure. Our research is significant not only because it identifies the novel protein components that make up the material within the AO that give it its structure but also because we find that the\n            <jats:named-content content-type=\"genus-species\">M. penetrans<\/jats:named-content>\n            AO is organized unlike AOs from other mycoplasmas, suggesting that similar structures have evolved multiple times. From this work, we derive some basic principles by which mycoplasmas, and potentially all organisms, build structures at the subcellular level.\n          <\/jats:p>","DOI":"10.1128\/jb.00069-17","type":"journal-article","created":{"date-parts":[[2017,4,4]],"date-time":"2017-04-04T00:30:45Z","timestamp":1491265845000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":18,"title":["The Variable Internal Structure of the Mycoplasma penetrans Attachment Organelle Revealed by Biochemical and Microscopic Analyses: Implications for Attachment Organelle Mechanism and Evolution"],"prefix":"10.1128","volume":"199","author":[{"given":"Steven L.","family":"Distelhorst","sequence":"first","affiliation":[{"name":"Department of Microbiology, Miami University, Oxford, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominika A.","family":"Jurkovic","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Miami University, Oxford, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jian","family":"Shi","sequence":"additional","affiliation":[{"name":"Division of Biology and Bioengineering, California Institute of Technology, Pasadena, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Grant J.","family":"Jensen","sequence":"additional","affiliation":[{"name":"Division of Biology and Bioengineering, California Institute of Technology, Pasadena, California, USA"},{"name":"Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mitchell F.","family":"Balish","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Miami University, Oxford, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.2741\/1943"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01865-14"},{"key":"e_1_3_3_4_2","first-page":"1","volume-title":"Molecular biology and pathogenicity of mycoplasmas","author":"Johannson KE","year":"2002","unstructured":"Johannson KE Pettersson B . 2002. 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