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(Створена сторінка: burgdorferi interactions with all the host ECM are for that reason probably critical in each the spirochete's pathogenesis too as its persistence in mammals. B....)
 
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burgdorferi interactions with all the host ECM are for that reason probably critical in each the spirochete's pathogenesis too as its persistence in mammals. B. burgdorferi binds different components with the ECM, including glycosaminoglycans (GAGS), fibronectin, decorin, collagen, laminin, and [https://www.medchemexpress.com/Dolastatin-10.html DLS 10 web] integrins. Additionally, B. burgdorferi adheres to quite a few host cell kinds and binds elements of host serum and extracellular fluids, including plasminogen and complement regulators (Table 1). Several B. burgdorferi adhesins have been not too long ago reviewed by Antonara et al. (2011). Even so, considerable analysis in to the functions and biomolecular interactions of those adhesins has taken place due to the fact then, including the identification of novel Lyme spirochete adhesins. In this evaluation, we supply an update on B. burgdorferi adhesins, focusing particularly around the bacterial elements that interact with components [https://dx.doi.org/10.1016/j.cub.2015.05.021 title= j.cub.2015.05.021] in the ECM, plasminogen, and complement regulators. For readers enthusiastic about adhesins involved in spirochete/tick interactions, please refer towards the recent evaluation by Kung et al. (2013). We would also refer the reader for the excellent discussion of novel in vivo imaging strategies and their use in delineating the roles of B. burgdorferi adhesins inside a infectious mouse model in the operate of Coburn et al. (2013).Frontiers in Cellular and Infection Microbiologywww.frontiersin.orgApril 2014 | Volume four | Short article 41 |Brissette and GaultneyB. burgdorferi adhesinsTable 1 | B. burgdorferi adhesins.Function Adhesin (genetic locus) FIBRONECTIN BINDING BBK32 (bbk32) Also binds GAGs; mutants attenuated in mice; part in vascular interactions in mice Probert and Johnson, 1998; Probert et al., 2001; Kim et al., 2004; Raibaud et al., 2005; Fischer et al., 2006; Li et al., 2006; Seshu et al., 2006; Norman et al., 2008; Hyde et al., 2011; Chan et al., 2012; Lin et al., 2012; [https://www.medchemexpress.com/DMOG.html Dimethyloxallyl Glycine site] Moriarty et al., 2012 Gilmore and Mbow, 1998; Carroll et al., 2001; Mbow et al., 2002; Brissette et al., 2009a, 2010; Lin et al., 2012; Moriarty et al., 2012; Floden et al., 2013 Brissette et al., 2009a, 2010; Lin et al., 2012; Moriarty et al., 2012 Moriarty et al., 2012; Gaultney et al., 2013 Hallstrom et al., 2010 Hallstrom et al., 2010 Fischer et al., 2003; Shi et al., 2006; Blevins et al., 2008; Shi et al., 2008a,b; Benoit et al., 2011; Hyde et al., 2011; Chan et al., 2012; Lin et al., 2012; Wang, 2012; Imai et al., 2013; Morgan and Wang, 2013 Parveen et al., 2006; Lin et al., 2012 Coleman et al., 2013; Kariu et al., 2013; Russell and Johnson, 2013; Russell et al., 2013 Pal et al., 2008; Yang et al., 2008; Verma et al., 2009 Brissette et al., 2009c Also binds complement regulator proteins, plasminogen, fibronectin, [https://dx.doi.org/10.1371/journal.pone.0169185 title= journal.pone.0169185] others Also binds complement regulator proteins, plasminogen, fibronectin, other individuals Hallstrom et al., 2010 Hallstrom et al., 2010 CommentsWHY DATE THE TREE OF LIFE?A number of the most simple concerns regarding the evolution of life concern the chronology of events. When did a offered taxon seem? When did it diversify? Was its diversification slow and gradual, or did it take place in bursts (evolutionary radiations), and in that case, when have been these bursts, and what caused th.Rtz et al., 1992; Shih et al., 1992; Pachner et al., 1995; Coburn et al., 2002; Liveris et al., 2002; Miller et al., 2006; Bykowski et al., 2007).
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burgdorferi binds different components of the ECM, which includes glycosaminoglycans (GAGS), fibronectin, [http://bowfishingnation.com/members/shearsshrine65/activity/49391/ -coding sequences encompass that influence autoimmunity. For example, miRNAs miR-23b] decorin, collagen, laminin, and integrins. When did a offered taxon appear? When did it diversify? Was its diversification slow and gradual, or did it occur in bursts (evolutionary radiations), and if so, when had been these bursts, and what caused th.Rtz et al., 1992; Shih et al., 1992; Pachner et al., 1995; Coburn et al., 2002; Liveris et al., 2002; Miller et al., 2006; Bykowski et al., 2007). Indeed, the ability of B. burgdorferi to invade collagenous tissue has been recommended as a possible mechanism of immune evasion (Cadavid et al., 2003; Barthold et al., 2006; Cabello et al., 2007). B. burgdorferi interactions with the host ECM are consequently likely critical in both the spirochete's pathogenesis too as its persistence in mammals. B. burgdorferi binds various elements on the ECM, such as glycosaminoglycans (GAGS), fibronectin, decorin, collagen, laminin, and integrins. In addition, B. burgdorferi adheres to several host cell kinds and binds components of host serum and extracellular fluids, including plasminogen and complement regulators (Table 1). Quite a few B. burgdorferi adhesins were recently reviewed by Antonara et al. (2011). Having said that, considerable investigation into the functions and biomolecular interactions of those adhesins has taken spot given that then, like the identification of novel Lyme spirochete adhesins. In this critique, we offer an update on B. burgdorferi adhesins, focusing particularly on the bacterial elements that interact with components [https://dx.doi.org/10.1016/j.cub.2015.05.021 title= j.cub.2015.05.021] in the ECM, plasminogen, and complement regulators. For readers considering adhesins involved in spirochete/tick interactions, please refer for the recent overview by Kung et al. (2013). We would also refer the reader for the great discussion of novel in vivo imaging procedures and their use in delineating the roles of B. burgdorferi adhesins in a infectious mouse model in the perform of Coburn et al. (2013).Frontiers in Cellular and Infection Microbiologywww.frontiersin.orgApril 2014 | Volume four | Short article 41 |Brissette and GaultneyB. burgdorferi adhesinsTable 1 | B. burgdorferi adhesins.Function Adhesin (genetic locus) FIBRONECTIN BINDING BBK32 (bbk32) Also binds GAGs; mutants attenuated in mice; function in vascular interactions in mice Probert and Johnson, 1998; Probert et al., 2001; Kim et al., 2004; Raibaud et al., 2005; Fischer et al., 2006; Li et al., 2006; Seshu et al., 2006; Norman et al., 2008; Hyde et al., 2011; Chan et al., 2012; Lin et al., 2012; Moriarty et al., 2012 Gilmore and Mbow, 1998; Carroll et al., 2001; Mbow et al., 2002; Brissette et al., 2009a, 2010; Lin et al., 2012; Moriarty et al., 2012; Floden et al., 2013 Brissette et al., 2009a, 2010; Lin et al., 2012; Moriarty et al., 2012 Moriarty et al., 2012; Gaultney et al., 2013 Hallstrom et al., 2010 Hallstrom et al., 2010 Fischer et al., 2003; Shi et al., 2006; Blevins et al., 2008; Shi et al., 2008a,b; Benoit et al., 2011; Hyde et al., 2011; Chan et al., 2012; Lin et al., 2012; Wang, 2012; Imai et al., 2013; Morgan and Wang, 2013 Parveen et al., 2006; Lin et al., 2012 Coleman et al., 2013; Kariu et al., 2013; Russell and Johnson, 2013; Russell et al., 2013 Pal et al., 2008; Yang et al., 2008; Verma et al., 2009 Brissette et al., 2009c Also binds complement regulator proteins, plasminogen, fibronectin, [https://dx.doi.org/10.1371/journal.pone.0169185 title= journal.pone.0169185] others Also binds complement regulator proteins, plasminogen, fibronectin, other individuals Hallstrom et al., 2010 Hallstrom et al., 2010 CommentsWHY DATE THE TREE OF LIFE?Many of the most simple queries in regards to the evolution of life concern the chronology of events.

Поточна версія на 09:22, 7 грудня 2017

burgdorferi binds different components of the ECM, which includes glycosaminoglycans (GAGS), fibronectin, -coding sequences encompass that influence autoimmunity. For example, miRNAs miR-23b decorin, collagen, laminin, and integrins. When did a offered taxon appear? When did it diversify? Was its diversification slow and gradual, or did it occur in bursts (evolutionary radiations), and if so, when had been these bursts, and what caused th.Rtz et al., 1992; Shih et al., 1992; Pachner et al., 1995; Coburn et al., 2002; Liveris et al., 2002; Miller et al., 2006; Bykowski et al., 2007). Indeed, the ability of B. burgdorferi to invade collagenous tissue has been recommended as a possible mechanism of immune evasion (Cadavid et al., 2003; Barthold et al., 2006; Cabello et al., 2007). B. burgdorferi interactions with the host ECM are consequently likely critical in both the spirochete's pathogenesis too as its persistence in mammals. B. burgdorferi binds various elements on the ECM, such as glycosaminoglycans (GAGS), fibronectin, decorin, collagen, laminin, and integrins. In addition, B. burgdorferi adheres to several host cell kinds and binds components of host serum and extracellular fluids, including plasminogen and complement regulators (Table 1). Quite a few B. burgdorferi adhesins were recently reviewed by Antonara et al. (2011). Having said that, considerable investigation into the functions and biomolecular interactions of those adhesins has taken spot given that then, like the identification of novel Lyme spirochete adhesins. In this critique, we offer an update on B. burgdorferi adhesins, focusing particularly on the bacterial elements that interact with components title= j.cub.2015.05.021 in the ECM, plasminogen, and complement regulators. For readers considering adhesins involved in spirochete/tick interactions, please refer for the recent overview by Kung et al. (2013). We would also refer the reader for the great discussion of novel in vivo imaging procedures and their use in delineating the roles of B. burgdorferi adhesins in a infectious mouse model in the perform of Coburn et al. (2013).Frontiers in Cellular and Infection Microbiologywww.frontiersin.orgApril 2014 | Volume four | Short article 41 |Brissette and GaultneyB. burgdorferi adhesinsTable 1 | B. burgdorferi adhesins.Function Adhesin (genetic locus) FIBRONECTIN BINDING BBK32 (bbk32) Also binds GAGs; mutants attenuated in mice; function in vascular interactions in mice Probert and Johnson, 1998; Probert et al., 2001; Kim et al., 2004; Raibaud et al., 2005; Fischer et al., 2006; Li et al., 2006; Seshu et al., 2006; Norman et al., 2008; Hyde et al., 2011; Chan et al., 2012; Lin et al., 2012; Moriarty et al., 2012 Gilmore and Mbow, 1998; Carroll et al., 2001; Mbow et al., 2002; Brissette et al., 2009a, 2010; Lin et al., 2012; Moriarty et al., 2012; Floden et al., 2013 Brissette et al., 2009a, 2010; Lin et al., 2012; Moriarty et al., 2012 Moriarty et al., 2012; Gaultney et al., 2013 Hallstrom et al., 2010 Hallstrom et al., 2010 Fischer et al., 2003; Shi et al., 2006; Blevins et al., 2008; Shi et al., 2008a,b; Benoit et al., 2011; Hyde et al., 2011; Chan et al., 2012; Lin et al., 2012; Wang, 2012; Imai et al., 2013; Morgan and Wang, 2013 Parveen et al., 2006; Lin et al., 2012 Coleman et al., 2013; Kariu et al., 2013; Russell and Johnson, 2013; Russell et al., 2013 Pal et al., 2008; Yang et al., 2008; Verma et al., 2009 Brissette et al., 2009c Also binds complement regulator proteins, plasminogen, fibronectin, title= journal.pone.0169185 others Also binds complement regulator proteins, plasminogen, fibronectin, other individuals Hallstrom et al., 2010 Hallstrom et al., 2010 CommentsWHY DATE THE TREE OF LIFE?Many of the most simple queries in regards to the evolution of life concern the chronology of events.