2b4h: Difference between revisions

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==Overview==

The spike protein VP4 is a key component of the membrane penetration, apparatus of rotavirus, a nonenveloped virus that causes childhood, gastroenteritis. Trypsin cleavage of VP4 produces a fragment, VP5*, with a, potential membrane interaction region, and primes rotavirus for cell, entry. During entry, the part of VP5* that protrudes from the virus folds, back on itself and reorganizes from a local dimer to a trimer. Here, we, report that a globular domain of VP5*, the VP5* antigen domain, is an, autonomously folding unit that alternatively forms well-ordered dimers and, trimers. Because the domain contains heterotypic neutralizing epitopes and, is soluble when expressed directly, it is a promising potential subunit, vaccine component. X-ray crystal structures show that the dimer resembles, the spike body on trypsin-primed virions, and the trimer resembles the, folded-back form of the spike. The same structural elements pack, differently to form key intermolecular contacts in both oligomers. The, intrinsic molecular property of alternatively forming dimers and trimers, facilitates the VP5* reorganization, which is thought to mediate membrane, penetration during cell entry.

The spike protein VP4 is a key component of the membrane penetration apparatus of rotavirus, a nonenveloped virus that causes childhood gastroenteritis. Trypsin cleavage of VP4 produces a fragment, VP5*, with a potential membrane interaction region, and primes rotavirus for cell entry. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. Here, we report that a globular domain of VP5*, the VP5* antigen domain, is an autonomously folding unit that alternatively forms well-ordered dimers and trimers. Because the domain contains heterotypic neutralizing epitopes and is soluble when expressed directly, it is a promising potential subunit vaccine component. X-ray crystal structures show that the dimer resembles the spike body on trypsin-primed virions, and the trimer resembles the folded-back form of the spike. The same structural elements pack differently to form key intermolecular contacts in both oligomers. The intrinsic molecular property of alternatively forming dimers and trimers facilitates the VP5* reorganization, which is thought to mediate membrane penetration during cell entry.

==About this Structure==

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[[Category: Rhesus rotavirus]]

[[Category: Single protein]]

[[Category: Dormitzer, P.R.]]

[[Category: Dormitzer, P R.]]

[[Category: Yoder, J.D.]]

[[Category: Yoder, J D.]]

[[Category: MPD]]

[[Category: TRS]]

[[Category: beta sandwich; greek key; membrane penetration protein; non-enveloped virus; spike protein; rearrangement]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The spike protein VP4 is a key component of the membrane penetration, apparatus of rotavirus, a nonenveloped virus that causes childhood, gastroenteritis. Trypsin cleavage of VP4 produces a fragment, VP5*, with a, potential membrane interaction region, and primes rotavirus for cell, entry. During entry, the part of VP5* that protrudes from the virus folds, back on itself and reorganizes from a local dimer to a trimer. Here, we, report that a globular domain of VP5*, the VP5* antigen domain, is an, autonomously folding unit that alternatively forms well-ordered dimers and, trimers. Because the domain contains heterotypic neutralizing epitopes and, is soluble when expressed directly, it is a promising potential subunit, vaccine component. X-ray crystal structures show that the dimer resembles, the spike body on trypsin-primed virions, and the trimer resembles the, folded-back form of the spike. The same structural elements pack, differently to form key intermolecular contacts in both oligomers. The, intrinsic molecular property of alternatively forming dimers and trimers, facilitates the VP5* reorganization, which is thought to mediate membrane, penetration during cell entry.
+The spike protein VP4 is a key component of the membrane penetration apparatus of rotavirus, a nonenveloped virus that causes childhood gastroenteritis. Trypsin cleavage of VP4 produces a fragment, VP5*, with a potential membrane interaction region, and primes rotavirus for cell entry. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. Here, we report that a globular domain of VP5*, the VP5* antigen domain, is an autonomously folding unit that alternatively forms well-ordered dimers and trimers. Because the domain contains heterotypic neutralizing epitopes and is soluble when expressed directly, it is a promising potential subunit vaccine component. X-ray crystal structures show that the dimer resembles the spike body on trypsin-primed virions, and the trimer resembles the folded-back form of the spike. The same structural elements pack differently to form key intermolecular contacts in both oligomers. The intrinsic molecular property of alternatively forming dimers and trimers facilitates the VP5* reorganization, which is thought to mediate membrane penetration during cell entry.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Rhesus rotavirus]]
 [[Category: Single protein]]
-[[Category: Dormitzer, P.R.]]
+[[Category: Dormitzer, P R.]]
-[[Category: Yoder, J.D.]]
+[[Category: Yoder, J D.]]
 [[Category: MPD]]
 [[Category: TRS]]
 [[Category: beta sandwich; greek key; membrane penetration protein; non-enveloped virus; spike protein; rearrangement]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:16:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:04 2008''