Sandbox ASBMB 3 - Revision history

Student at 22:31, 7 August 2009

2009-08-07T22:31:28Z

←Older revision		Revision as of 22:31, 7 August 2009
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	Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.		Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.

-	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry [[3cl0]]). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.	+	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a <scene name='Sandbox_ASBMB_3/Tamiflu_glu_his/1'>common mutant</scene> (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry [[3cl0]]). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.

	<quiz display=simple>		<quiz display=simple>

Student at 22:05, 7 August 2009

2009-08-07T22:05:59Z

←Older revision		Revision as of 22:05, 7 August 2009
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-
	== Influenza neuraminidase ==		== Influenza neuraminidase ==
-		+	<applet load='3cl0' size='300' frame='true' align='right' caption='Insert caption here' />

	Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.		Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.

Student at 22:00, 7 August 2009

2009-08-07T22:00:24Z

←Older revision		Revision as of 22:00, 7 August 2009
Line 1:		Line 1:
-	Influenza neuraminidase	+
		+	== Influenza neuraminidase ==
		+

	Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.		Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.

-	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry 3cl0). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.	+	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry [[3cl0]]). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.

	<quiz display=simple>		<quiz display=simple>

Eran Hodis at 03:00, 7 August 2009

2009-08-07T03:00:20Z

←Older revision		Revision as of 03:00, 7 August 2009
Line 1:		Line 1:
-	== Influenza neuraminidase ==	+	Influenza neuraminidase

-	<applet load='3cl0' size='300' frame='true' align='right' caption='Insert caption here' />
	Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.		Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.

-	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a ~~<scene name='Sandbox_ASBMB_3/3cl0_tamiflu_highlighted/1'>~~common mutant~~</scene>~~ (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry [[3cl0]]). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.	+	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry 3cl0). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.

	<quiz display=simple>		<quiz display=simple>

Student at 22:35, 6 August 2009

2009-08-06T22:35:19Z

←Older revision		Revision as of 22:35, 6 August 2009
Line 4:		Line 4:
	Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.		Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.

-	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry [[3cl0]]). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.	+	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a <scene name='Sandbox_ASBMB_3/3cl0_tamiflu_highlighted/1'>common mutant</scene> (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry [[3cl0]]). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.

	<quiz display=simple>		<quiz display=simple>

Student at 22:17, 6 August 2009

2009-08-06T22:17:45Z

←Older revision		Revision as of 22:17, 6 August 2009
Line 1:		Line 1:
-
	== Influenza neuraminidase ==		== Influenza neuraminidase ==

-		+	<applet load='3cl0' size='300' frame='true' align='right' caption='Insert caption here' />
	Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.		Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.

Student at 22:14, 6 August 2009

2009-08-06T22:14:07Z

←Older revision		Revision as of 22:14, 6 August 2009
Line 1:		Line 1:
-	Influenza neuraminidase	+
		+	== Influenza neuraminidase ==
		+

	Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.		Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.

-	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry 3cl0). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.	+	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry [[3cl0]]). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.

	<quiz display=simple>		<quiz display=simple>

Eran Hodis at 16:00, 6 August 2009

2009-08-06T16:00:26Z

←Older revision		Revision as of 16:00, 6 August 2009
Line 3:		Line 3:
	Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.		Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.

-	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu, resulting in weaker drug binding and thus resistance (PDB entry 3cl0). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.	+	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu binding, resulting in weaker drug binding and thus resistance (PDB entry 3cl0). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.

	<quiz display=simple>		<quiz display=simple>

Eran Hodis at 14:25, 4 August 2009

2009-08-04T14:25:03Z

←Older revision		Revision as of 14:25, 4 August 2009
Line 3:		Line 3:
	Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.		Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.

-	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza)~~. Unfortunately, by early 2009, 98% of influenza A/H1N1 strains in North America have become resistant to Tamiflu~~. Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu, resulting in weaker drug binding and thus resistance (PDB entry 3cl0). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.	+	Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu, resulting in weaker drug binding and thus resistance (PDB entry 3cl0). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.

	<quiz display=simple>		<quiz display=simple>

Eran Hodis: New page: Influenza neuraminidase Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new ...

2009-08-04T13:30:19Z

New page: Influenza neuraminidase Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new ...

New page

Influenza neuraminidase

Influenza '''neuraminidase''' is a glycoprotein in the influenza virus membrane. Before an infected cell can release the virus into its surroundings to infect new cells, neuraminidase must cleave sialic acid from both virus and cellular glycoproteins.

Because of its important role in virus infectivity, several anti-viral drugs have been designed to target neuraminidase, including oseltamivir (Tamiflu) and zanamivir (Relenza). Unfortunately, by early 2009, 98% of influenza A/H1N1 strains in North America have become resistant to Tamiflu. Tamiflu binding to neuraminidase moves glutamate 276 towards histidine 274, making more room for Tamiflu to bind tightly (PDB entry [[2hu4]]). But, in a common mutant (H274Y), a larger tyrosine replaces the smaller histidine 274, preventing glutamate 276 from moving to make room for Tamiflu, resulting in weaker drug binding and thus resistance (PDB entry 3cl0). Luckily the H274Y neuraminidase mutant is still susceptible to Relenza, which is smaller than Tamiflu.

<quiz display=simple>
{Which neuraminidase residue moves to make room for Tamiflu binding but cannot do so in the H274Y neuraminidase mutant?
|type="[]"}
- histidine 274
- serine 278
+ glutamate 276
- tyrosine 274
</quiz>