Contido eliminado Contido engadido
== Estruturas ==
No decurso da [[evolución]] distintas especies de bacterias desenvoloveron diferentes solucións ao problema de unirse a proteínas receptoras específicas da superficie celular. Actualmente coñécense varios tipos e subclases de adhesinas bacterianas.
Through the mechanisms of evolution, different species of bacteria have developed different solutions to the problem of attaching receptor specific proteins to the bacteria surface. Today many different types and subclasses of bacterial adhesins may be observed in the literature.
TheA typicalestrutura structuretípìca ofdunha aadhesión bacterialbacteriana adhesioné isa that of adunha [[fimbria (bacteriology)|fimbria]] orou [[pilus|pili]].<ref name=Per_Klem_2000 /> TheA bacterialadhesión adhesionbacteriana consistsconsiste primarilyprincipalmente ofnunha anproteína intramembranousestrutural structuralintramembranosa proteinque whichserve providesde aarmazón scaffoldno uponcal whichse severalpoden extracellularunir adhesinsvarias mayadhesinas be attachedextracelulares .<ref name=Per_Klem_2000 /> HoweverPorén , ascomo inocorre theno casecaso ofdas thefimbrias CFA1 fimbriae, thea structuralproteína proteinestrutural itselfpor cansi sometimessoa actpode asás anveces adhesionactuar ifcomo aunha portionadhesión ofse theunha proteinporción extendsda intoproteína the se estende pola [[extramatriz cellular matrix|ECMextracelular ]].
=== Estrutura da adhesina FimH ===
===FimH Adhesin — Structure===
TheA bestadhesina characterizedbacteriana bacterialmellor adhesincracterizada isé thea typeadhesina 1FimH fimbrialde FimHfimbria adhesinde tipo 1 . ThisEsta adhesinadhesina isé responsibleresponsable forda adhesión sensible a [[mannosemanosa |D-mannosemanosa ]] sensitive adhesion.<ref name=Per_Klem_2000 /> TheA bacteriumbacteria synthesizessintetiza aunha precursorproteína proteinprecursora consistingque ofconsta de 300 [[amino acidaminoácido ]]s thendespois processesprocesa thea proteinproteína byeliminando removingvarios several[[péptido signalsinal|péptidos peptidessinais]] ultimatelyquedando leavingfinalmete aunha 279proteína aminode acid279 proteinaminoácidos .<ref name=Per_Klem_2000 /> Mature FimH is displayed on the bacterial surface as a component of the type 1 fimbrial organelle.<ref name=Per_Klem_2000 />
InEn 1999, thea structureestrutura ofde FimH wasfoi resolvedresolta viapo [[x-raycristalografía crystallographyde raios X ]]. FimH isestá foldedpregada intoen twodous domains[[dominio proteico|dominios]] . TheO Ndominio adhesivo N- terminal adhesiveé domaino playsque thedesempeña maino rolepe¡apel inprincipal surfacebo recognitionrecoñecemento whilede thesuperficies, mentres que o dominio C-terminal domainé isresponsable responsibleda forintegración organelleen integration[[orgánulo]]s .<ref name=Choudhury>{{cite journal |author=Choudhury D, Thompson A, Stojanoff V |title=X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic ''Escherichia coli'' |journal=Science |volume=285 |issue=5430 |pages=1061–6 |date=August 1999 |pmid=10446051 |url=http://www.sciencemag.org/cgi/pmidlookup?view=long&pmid=10446051 |doi=10.1126/science.285.5430.1061|display-authors=etal}}</ref> AUn [[turnxiro (biochemistrybioquímica )|tetra-peptidebucle looptetrapéptido ]] linksune theos twodous domainsdominios . AdditionallyAdemais , aidentificouse carbohydrate-bindingun pocketpeto hasde beenunión identifieda atcarbohidratos theno tipextremo ofdo thedominio adhesivo N-terminal adhesive domain.<ref name=Choudhury /> ThisEsrta basicestrutura structurebásica isestá conservedconservada acrossentre typeas adhesinas de fimbria de tipo 1, fimbrialaínda adhesinsque thoughestudos recentrecentes studiesmostraron haveque shownas thatmutacións inducidas [[ in vitro]] inducedpoden mutationsorixinar cana leadadición tode theespecificidade additionno ofdominio C-terminal, domaino specificityque resultingdá inlugar a bacterialunha adhesionadhesión withbacteriana dualcon bendingdous sitessitios andde unión e [[fenotipo]]s relatedde bindingunión phenotypesrelacionados .<ref name=Schembri>{{cite journal |author=Schembri MA, Klemm P |title=Heterobinary adhesins based on the ''Escherichia coli'' FimH fimbrial protein |journal=Appl. Environ. Microbiol. |volume=64 |issue=5 |pages=1628–33 |date=May 1998 |pmid=9572927 |pmc=106206 |url=http://aem.asm.org/cgi/pmidlookup?view=long&pmid=9572927}}</ref>
== As adhesinas como factores de virulencia ==
