Editing Mycoplasma genitalium (section)

==Research==
The discovery of [[Protein M]], a protein produced by ''M. genitalium'', was announced in February 2014.<ref name=scripps>{{cite web |title=The Ultimate Decoy: Scripps Research Institute Scientists Find Protein that Helps Bacteria Misdirect Immune System |url=http://www.scripps.edu/news/press/2014/20140206lerner.html |publisher=The Scripps Research Institute (TSRI) |access-date=9 August 2014 |archive-date=4 June 2014 |archive-url=https://web.archive.org/web/20140604001536/http://www.scripps.edu/news/press/2014/20140206lerner.html |url-status=live }}</ref> The protein was identified during investigations on the origin of [[multiple myeloma]], a B-cell hematologic neoplasm. To understand the long-term ''Mycoplasma'' infection, it was found that [[antibodies]] from multiple myeloma patients' blood were recognised by ''M. genitalium''. The antibody reactivity was due to a protein, designated Protein M, that is chemically responsive to all types of human and nonhuman antibodies available. The protein is about 50 kDa in size, and composed of 556 amino acids.<ref>{{cite journal |last1=Grover |first1=R. K. |last2=Zhu |first2=X. |last3=Nieusma |first3=T. |last4=Jones |first4=T. |last5=Boero |first5=I. |last6=MacLeod |first6=A. S. |last7=Mark |first7=A. |last8=Niessen |first8=S. |last9=Kim |first9=H. J.|last10=Kong|first10=L. |last11=Assad-Garcia |first11=N. |last12=Kwon |first12=K. |last13=Chesi |first13=M. |last14=Smider |first14=V. V. |last15=Salomon |first15=D. R. |last16=Jelinek |first16=D. F. |last17=Kyle |first17=R. A. |last18=Pyles |first18=R. B. |last19=Glass |first19=J. I.|last20=Ward|first20=A. B. |last21=Wilson |first21=I. A. |last22=Lerner |first22=R. A. |title=A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union |journal=Science |date=2014 |volume=343 |issue=6171 |pages=656–661 |doi=10.1126/science.1246135 |pmid=24503852 |pmc=3987992 |bibcode=2014Sci...343..656G}}</ref>

Mgen evolved from a gram-positive ancestor that was clostridium-like but has lost the genes to code for the enzymes involved in de novo nucleic acid synthesis, amino acid synthesis, and synthesis of fatty acids.<ref>{{cite journal |last1=Raj |first1=Stephen |title=Mycoplasma genitalium : A new superbug |journal=Indian Journal of Sexually Transmitted Diseases and AIDS |date=2022 |volume=43 |issue=2589–0557|pages=1–12 |doi=10.4103/ijstd.ijstd_103_20 |doi-access=free |pmid=35846530 |pmc=9282694 }}</ref> This means that Mgen needs the host's growth factors to keep reproducing. Although Mgen has abilities that help it adhere to cells, it is still unknown how the bacteria can maintain an infection inside the epithelial cells of the ectocervix and vagina when shedding of the apical layer of cells occur. The organism's ability to have adhesion to host cells relies of two proteins, P110 and P140. Adhesion is an important step in beginning an infection in a cell and Mgen can adhere to spermatozoa, erythrocytes, and epithelial cells. The terminal organelle relies on these proteins as well because without them the organelle was not present. The segmented pair plates of Mgen {{vague|date=November 2023}} is a core of dense electrons which is anchored to the cell membrane. The end of this core is in contact with the wheel complex and the wheel complex contains the proteins MG219, MG200, MG386, and MG491 which aid in the gliding motility of the bacteria. Although Mgen lacks secreted virulence factors, the protein MG186 degrades host nucleic acids due to it being a calcium-dependent membrane-associated nuclease.{{fact|date=November 2023}}