OspC and Binding - Revision history

Alexander Berchansky at 10:57, 13 September 2012

Alexander Berchansky — Thu, 13 Sep 2012 10:57:06 GMT

←Older revision		Revision as of 10:57, 13 September 2012
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	==See also==		==See also==
-	Outer surface protein	+	[[Outer surface protein]]

Alexander Berchansky at 10:56, 13 September 2012

Alexander Berchansky — Thu, 13 Sep 2012 10:56:47 GMT

←Older revision		Revision as of 10:56, 13 September 2012
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	<ref group="xtra">PMID:11901105</ref><references group="xtra"/>		<ref group="xtra">PMID:11901105</ref><references group="xtra"/>
		+
		+	==See also==
		+	Outer surface protein

Michal Harel at 09:28, 12 August 2012

Michal Harel — Sun, 12 Aug 2012 09:28:40 GMT

←Older revision		Revision as of 09:28, 12 August 2012
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-	<applet load='1GGQ' size='500' frame='true' align='right' caption='Outer Surface Protein C of the B. burgdorferi spirochete.' scene= />	+	<applet load='1GGQ' size='500' frame='true' align='right' caption='Outer Surface Protein C of the B. burgdorferi spirochete complex with Mg+2 ion [[1ggq]]' scene= />

	The '''outer surface protein C''' (ospC) is a major antigen on the outer surface of the membrane of[http://en.wikipedia.org/wiki/Borrelia_burgdorferi '' B. burgdorferi''], the [http://en.wikipedia.org/wiki/Spirochete spirochete] that causes [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease]. Although its main functions are largely unknown, ospC’s large degree of [http://en.wikipedia.org/wiki/Polymorphism_%28biology%29 polymorphism] allows it to be an effective tool in [http://en.wikipedia.org/wiki/Epidemiology epidemiology] and [http://en.wikipedia.org/wiki/Ecology ecology]. The different alleles coding for different types of groups of ospC’s are called ospC Major Groups (oMG’s). There are approximately 19 oMG’s, four of which—oMG’s A, B, I, and K—are virulent to humans (Kumaran et al. 2001). Research has found that infection rates of susceptible hosts to virulent oMG’s are higher where genetic variation is low due to [http://en.wikipedia.org/wiki/Population_bottleneck bottleneck effects] in certain regions of the world, such as the northeastern United States and parts of Europe (Wei-Gang et al. 2002). However, rarer oMG’s also hold a selective advantage in subsequent infections of a host, as the host’s strong secondary response would prevent infection from an oMG to which it has already been exposed (Brisson et al. 2002).		The '''outer surface protein C''' (ospC) is a major antigen on the outer surface of the membrane of[http://en.wikipedia.org/wiki/Borrelia_burgdorferi '' B. burgdorferi''], the [http://en.wikipedia.org/wiki/Spirochete spirochete] that causes [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease]. Although its main functions are largely unknown, ospC’s large degree of [http://en.wikipedia.org/wiki/Polymorphism_%28biology%29 polymorphism] allows it to be an effective tool in [http://en.wikipedia.org/wiki/Epidemiology epidemiology] and [http://en.wikipedia.org/wiki/Ecology ecology]. The different alleles coding for different types of groups of ospC’s are called ospC Major Groups (oMG’s). There are approximately 19 oMG’s, four of which—oMG’s A, B, I, and K—are virulent to humans (Kumaran et al. 2001). Research has found that infection rates of susceptible hosts to virulent oMG’s are higher where genetic variation is low due to [http://en.wikipedia.org/wiki/Population_bottleneck bottleneck effects] in certain regions of the world, such as the northeastern United States and parts of Europe (Wei-Gang et al. 2002). However, rarer oMG’s also hold a selective advantage in subsequent infections of a host, as the host’s strong secondary response would prevent infection from an oMG to which it has already been exposed (Brisson et al. 2002).

Michal Harel at 09:25, 12 August 2012

Michal Harel — Sun, 12 Aug 2012 09:25:22 GMT

←Older revision		Revision as of 09:25, 12 August 2012
Line 5:		Line 5:
	<applet load='1GGQ' size='500' frame='true' align='right' caption='Outer Surface Protein C of the B. burgdorferi spirochete.' scene= />		<applet load='1GGQ' size='500' frame='true' align='right' caption='Outer Surface Protein C of the B. burgdorferi spirochete.' scene= />

-	The outer surface protein C (ospC) is a major antigen on the outer surface of the membrane of[http://en.wikipedia.org/wiki/Borrelia_burgdorferi '' B. burgdorferi''], the [http://en.wikipedia.org/wiki/Spirochete spirochete] that causes [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease]. Although its main functions are largely unknown, ospC’s large degree of [http://en.wikipedia.org/wiki/Polymorphism_%28biology%29 polymorphism] allows it to be an effective tool in [http://en.wikipedia.org/wiki/Epidemiology epidemiology] and [http://en.wikipedia.org/wiki/Ecology ecology]. The different alleles coding for different types of groups of ospC’s are called ospC Major Groups (oMG’s). There are approximately 19 oMG’s, four of which—oMG’s A, B, I, and K—are virulent to humans (Kumaran et al. 2001). Research has found that infection rates of susceptible hosts to virulent oMG’s are higher where genetic variation is low due to [http://en.wikipedia.org/wiki/Population_bottleneck bottleneck effects] in certain regions of the world, such as the northeastern United States and parts of Europe (Wei-Gang et al. 2002). However, rarer oMG’s also hold a selective advantage in subsequent infections of a host, as the host’s strong secondary response would prevent infection from an oMG to which it has already been exposed (Brisson et al. 2002).	+	The '''outer surface protein C''' (ospC) is a major antigen on the outer surface of the membrane of[http://en.wikipedia.org/wiki/Borrelia_burgdorferi '' B. burgdorferi''], the [http://en.wikipedia.org/wiki/Spirochete spirochete] that causes [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease]. Although its main functions are largely unknown, ospC’s large degree of [http://en.wikipedia.org/wiki/Polymorphism_%28biology%29 polymorphism] allows it to be an effective tool in [http://en.wikipedia.org/wiki/Epidemiology epidemiology] and [http://en.wikipedia.org/wiki/Ecology ecology]. The different alleles coding for different types of groups of ospC’s are called ospC Major Groups (oMG’s). There are approximately 19 oMG’s, four of which—oMG’s A, B, I, and K—are virulent to humans (Kumaran et al. 2001). Research has found that infection rates of susceptible hosts to virulent oMG’s are higher where genetic variation is low due to [http://en.wikipedia.org/wiki/Population_bottleneck bottleneck effects] in certain regions of the world, such as the northeastern United States and parts of Europe (Wei-Gang et al. 2002). However, rarer oMG’s also hold a selective advantage in subsequent infections of a host, as the host’s strong secondary response would prevent infection from an oMG to which it has already been exposed (Brisson et al. 2002).

	As a kidney-shaped structure with 174 amino acid residues, the ospC is a tetramer composed of two dimers. Most of the structure consists of <scene name='User:Gayatri_Setia/Workbench/Alpha_helices/2'>alpha helices</scene>, which are colored purple in the constructed model of <scene name='User:Gayatri_Setia/Workbench/Chain_a/2'>Chain A</scene>. There is only one <scene name='User:Gayatri_Setia/Workbench/Beta_sheet/1'>ß-pleated sheet</scene> on Chain A, marked in yellow.		As a kidney-shaped structure with 174 amino acid residues, the ospC is a tetramer composed of two dimers. Most of the structure consists of <scene name='User:Gayatri_Setia/Workbench/Alpha_helices/2'>alpha helices</scene>, which are colored purple in the constructed model of <scene name='User:Gayatri_Setia/Workbench/Chain_a/2'>Chain A</scene>. There is only one <scene name='User:Gayatri_Setia/Workbench/Beta_sheet/1'>ß-pleated sheet</scene> on Chain A, marked in yellow.

Emily Littman at 18:45, 24 April 2012

Emily Littman — Tue, 24 Apr 2012 18:45:19 GMT

←Older revision		Revision as of 18:45, 24 April 2012
Line 1:		Line 1:
		+	== OspC and Binding ==
		+
		+
		+
		+	<applet load='1GGQ' size='500' frame='true' align='right' caption='Outer Surface Protein C of the B. burgdorferi spirochete.' scene= />
		+
		+	The outer surface protein C (ospC) is a major antigen on the outer surface of the membrane of[http://en.wikipedia.org/wiki/Borrelia_burgdorferi '' B. burgdorferi''], the [http://en.wikipedia.org/wiki/Spirochete spirochete] that causes [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease]. Although its main functions are largely unknown, ospC’s large degree of [http://en.wikipedia.org/wiki/Polymorphism_%28biology%29 polymorphism] allows it to be an effective tool in [http://en.wikipedia.org/wiki/Epidemiology epidemiology] and [http://en.wikipedia.org/wiki/Ecology ecology]. The different alleles coding for different types of groups of ospC’s are called ospC Major Groups (oMG’s). There are approximately 19 oMG’s, four of which—oMG’s A, B, I, and K—are virulent to humans (Kumaran et al. 2001). Research has found that infection rates of susceptible hosts to virulent oMG’s are higher where genetic variation is low due to [http://en.wikipedia.org/wiki/Population_bottleneck bottleneck effects] in certain regions of the world, such as the northeastern United States and parts of Europe (Wei-Gang et al. 2002). However, rarer oMG’s also hold a selective advantage in subsequent infections of a host, as the host’s strong secondary response would prevent infection from an oMG to which it has already been exposed (Brisson et al. 2002).
		+
		+	As a kidney-shaped structure with 174 amino acid residues, the ospC is a tetramer composed of two dimers. Most of the structure consists of <scene name='User:Gayatri_Setia/Workbench/Alpha_helices/2'>alpha helices</scene>, which are colored purple in the constructed model of <scene name='User:Gayatri_Setia/Workbench/Chain_a/2'>Chain A</scene>. There is only one <scene name='User:Gayatri_Setia/Workbench/Beta_sheet/1'>ß-pleated sheet</scene> on Chain A, marked in yellow.
		+
		+	As ospC synthesis is increased upon transfer to a host, possibly due to a temperature increase, there is a possibility of a direct interaction between the ospC and the host (Kumaran et al. 2011). There is a higher density of <scene name='User:Gayatri_Setia/Workbench/Negative_charge_distribution/1'>negatively charged amino acids</scene>—marked in red—on one side of each dimer of virulent oMG’s than there is in non-virulent oMG’s (Fig. 1), which suggests a possible binding site for ospC with positively charged host-ligands.
		+
		+	[[Image:Fig_1.jpg]]
		+
		+	Fig. 1 shows the electrostatic surface potential map of A(HB19) and B(212). HB19 is a virulent strain from oMG A, and 212 is from a non-virulent strain. (Source: Kumaran et al. 2001)
		+
	== References ==		== References ==

Gayatri Setia: Replacing page with '== References == PMID:16606995 PMID:15514047 PMID:11230...'

Gayatri Setia — Tue, 24 Apr 2012 18:44:13 GMT

Replacing page with '== References == <ref group="xtra">PMID:16606995</ref><references group="xtra"/> <ref group="xtra">PMID:15514047</ref><references group="xtra"/> <ref group="xtra">PMID:11230...'

←Older revision		Revision as of 18:44, 24 April 2012
Line 1:		Line 1:
-	== OspC and Binding ==
-
-
-
-	<applet load='1GGQ' size='500' frame='true' align='right' caption='Outer Surface Protein C of the B. burgdorferi spirochete.' scene= />
-
-	The outer surface protein C (ospC) is a major antigen on the outer surface of the membrane of[http://en.wikipedia.org/wiki/Borrelia_burgdorferi '' B. burgdorferi''], the [http://en.wikipedia.org/wiki/Spirochete spirochete] that causes [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease]. Although its main functions are largely unknown, ospC’s large degree of [http://en.wikipedia.org/wiki/Polymorphism_%28biology%29 polymorphism] allows it to be an effective tool in [http://en.wikipedia.org/wiki/Epidemiology epidemiology] and [http://en.wikipedia.org/wiki/Ecology ecology]. The different alleles coding for different types of groups of ospC’s are called ospC Major Groups (oMG’s). There are approximately 19 oMG’s, four of which—oMG’s A, B, I, and K—are virulent to humans (Kumaran et al. 2001). Research has found that infection rates of susceptible hosts to virulent oMG’s are higher where genetic variation is low due to [http://en.wikipedia.org/wiki/Population_bottleneck bottleneck effects] in certain regions of the world, such as the northeastern United States and parts of Europe (Wei-Gang et al. 2002). However, rarer oMG’s also hold a selective advantage in subsequent infections of a host, as the host’s strong secondary response would prevent infection from an oMG to which it has already been exposed (Brisson et al. 2002).
-
-	As a kidney-shaped structure with 174 amino acid residues, the ospC is a tetramer composed of two dimers. Most of the structure consists of <scene name='User:Gayatri_Setia/Workbench/Alpha_helices/2'>alpha helices</scene>, which are colored purple in the constructed model of <scene name='User:Gayatri_Setia/Workbench/Chain_a/2'>Chain A</scene>. There is only one <scene name='User:Gayatri_Setia/Workbench/Beta_sheet/1'>ß-pleated sheet</scene> on Chain A, marked in yellow.
-
-	As ospC synthesis is increased upon transfer to a host, possibly due to a temperature increase, there is a possibility of a direct interaction between the ospC and the host (Kumaran et al. 2011). There is a higher density of <scene name='User:Gayatri_Setia/Workbench/Negative_charge_distribution/1'>negatively charged amino acids</scene>—marked in red—on one side of each dimer of virulent oMG’s than there is in non-virulent oMG’s (Fig. 1), which suggests a possible binding site for ospC with positively charged host-ligands.
-
-	[[Image:Fig_1.jpg]]
-
-	Fig. 1 shows the electrostatic surface potential map of A(HB19) and B(212). HB19 is a virulent strain from oMG A, and 212 is from a non-virulent strain. (Source: Kumaran et al. 2001)
-
	== References ==		== References ==

Gayatri Setia: New page: == OspC and Binding == The outer surface protein...
Gayatri Setia — Tue, 24 Apr 2012 18:42:32 GMT

New page: == OspC and Binding == <applet load='1GGQ' size='500' frame='true' align='right' caption='Outer Surface Protein C of the B. burgdorferi spirochete.' scene= /> The outer surface protein...

New page
== OspC and Binding ==

<applet load='1GGQ' size='500' frame='true' align='right' caption='Outer Surface Protein C of the B. burgdorferi spirochete.' scene= />

The outer surface protein C (ospC) is a major antigen on the outer surface of the membrane of[http://en.wikipedia.org/wiki/Borrelia_burgdorferi '' B. burgdorferi''], the [http://en.wikipedia.org/wiki/Spirochete spirochete] that causes [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease]. Although its main functions are largely unknown, ospC’s large degree of [http://en.wikipedia.org/wiki/Polymorphism_%28biology%29 polymorphism] allows it to be an effective tool in [http://en.wikipedia.org/wiki/Epidemiology epidemiology] and [http://en.wikipedia.org/wiki/Ecology ecology]. The different alleles coding for different types of groups of ospC’s are called ospC Major Groups (oMG’s). There are approximately 19 oMG’s, four of which—oMG’s A, B, I, and K—are virulent to humans (Kumaran et al. 2001). Research has found that infection rates of susceptible hosts to virulent oMG’s are higher where genetic variation is low due to [http://en.wikipedia.org/wiki/Population_bottleneck bottleneck effects] in certain regions of the world, such as the northeastern United States and parts of Europe (Wei-Gang et al. 2002). However, rarer oMG’s also hold a selective advantage in subsequent infections of a host, as the host’s strong secondary response would prevent infection from an oMG to which it has already been exposed (Brisson et al. 2002).

As a kidney-shaped structure with 174 amino acid residues, the ospC is a tetramer composed of two dimers. Most of the structure consists of <scene name='User:Gayatri_Setia/Workbench/Alpha_helices/2'>alpha helices</scene>, which are colored purple in the constructed model of <scene name='User:Gayatri_Setia/Workbench/Chain_a/2'>Chain A</scene>. There is only one <scene name='User:Gayatri_Setia/Workbench/Beta_sheet/1'>ß-pleated sheet</scene> on Chain A, marked in yellow.

As ospC synthesis is increased upon transfer to a host, possibly due to a temperature increase, there is a possibility of a direct interaction between the ospC and the host (Kumaran et al. 2011). There is a higher density of <scene name='User:Gayatri_Setia/Workbench/Negative_charge_distribution/1'>negatively charged amino acids</scene>—marked in red—on one side of each dimer of virulent oMG’s than there is in non-virulent oMG’s (Fig. 1), which suggests a possible binding site for ospC with positively charged host-ligands.

[[Image:Fig_1.jpg]]

Fig. 1 shows the electrostatic surface potential map of A(HB19) and B(212). HB19 is a virulent strain from oMG A, and 212 is from a non-virulent strain. (Source: Kumaran et al. 2001)

== References ==

<ref group="xtra">PMID:16606995</ref><references group="xtra"/>

<ref group="xtra">PMID:15514047</ref><references group="xtra"/>

<ref group="xtra">PMID:11230121</ref><references group="xtra"/>

<ref group="xtra">PMID:11901105</ref><references group="xtra"/>