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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">M-Protein</span></h1>
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<div id="mw-content-text" class="mw-body-content mw-content-ltr" lang="de" dir="ltr"><div class="mw-content-ltr mw-parser-output" lang="de" dir="ltr"><p>Als <b>M-Protein</b> bezeichnet man einen <a href="Virulenzfaktor" title="Virulenzfaktor">Virulenzfaktor</a> von <a href="Streptokokken" title="Streptokokken">Streptokokkenarten</a> der <a href="Lancefield-Einteilung" title="Lancefield-Einteilung">Lancefield-Einteilung-A</a> (Hauptvertreter: <i><a href="Streptococcus_pyogenes" title="Streptococcus pyogenes">Streptococcus pyogenes</a></i>). Es zählt zu den bedeutendsten <a href="Antigen" title="Antigen">Oberflächenantigenen</a> dieser Arten.
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<div class="mw-heading mw-heading2"><h2 id="Wirkmechanismus">Wirkmechanismus</h2></div>
<p>Aufgrund der Hemmung der Bindung von <a href="Leukozyt" title="Leukozyt">Leukozyten</a> an das Bakterium wirkt es stark antiphagozytär. Der Grund für die verminderte Bindung der Leukozyten besteht darin, dass das M-Protein die C3-Konvertase des <a href="Komplementsystem" title="Komplementsystem">Komplementsystems</a> zerstört. Folgend kann C3 nicht in C3a und C3b gespalten werden. C3b ist jedoch wichtig für die <a href="Opsonisierung" title="Opsonisierung">Opsonisierung</a>.
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<div class="mw-heading mw-heading2"><h2 id="Quellen">Quellen</h2></div>
<ul><li>N. Chanter, N. C. Talbot, J. R. Newton, D. Hewson, K. Verheyen: <i>Streptococcus equi with truncated M-proteins isolated from outwardly healthy horses.</i> In: <i>Microbiology.</i> 146 (Pt 6), Juni 2000, S. 1361–1369. <a href="https://doi.org/10.1099/00221287-146-6-1361" class="extiw external" title="doi:10.1099/00221287-146-6-1361">doi:10.1099/00221287-146-6-1361</a>. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/10846214?dopt=Abstract">PMID 10846214</a>.</li></ul>
<ul><li>O. Schneewind, K. F. Jones, V. A. Fischetti: <i>Sequence and structural characteristics of the trypsin-resistant T6 surface protein of group A streptococci.</i> In: <i>Journal of bacteriology.</i> Band 172, Nummer 6, Juni 1990, S. 3310–3317, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1128/jb.172.6.3310-3317.1990">10.1128/jb.172.6.3310-3317.1990</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/2188957?dopt=Abstract">PMID 2188957</a>, <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC209141/">PMC 209141</a> (freier Volltext).</li></ul>
<ul><li>V. A. Fischetti, V. Pancholi, O. Schneewind: <i>Conservation of a pentapeptide sequence in the anchor region of surface proteins from gram-positive cocci.</i> In: <i>Mol. Microbiol.</i> 4 (9), September 1990, S. 1603–1605. <a href="https://doi.org/10.1111/j.1365-2958.1990.tb02072.x" class="extiw external" title="doi:10.1111/j.1365-2958.1990.tb02072.x">doi:10.1111/j.1365-2958.1990.tb02072.x</a>. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/2287281?dopt=Abstract">PMID 2287281</a>.</li></ul>
<ul><li>V. A. Fischetti: <i>Streptococcal M protein: molecular design and biological behavior.</i> In: <i>Clin Microbiol Rev.</i> 2(3), Juli 1989, S. 285–314.</li></ul></div><!--htdig_noindex--><div><div class="zim-footer">
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