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Antigenic and 3D structural characterization of soluble X4 and hybrid X4-R5 HIV-1 Env trimers.
Arnold, Philipp Himmels, Patricia Weiß, Svenja Decker, Tim-Michael Markl, Jürgen Gatterdam, Volker Tampé, Robert Bartholomäus, Patrick Dietrich, Ursula Dürr, Ralf
Arnold, Philipp
Himmels, Patricia
Weiß, Svenja
Decker, Tim-Michael
Markl, Jürgen
Gatterdam, Volker
Tampé, Robert
Bartholomäus, Patrick
Dietrich, Ursula
Dürr, Ralf
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Abstract
HIV-1 is decorated with trimeric glycoprotein spikes that enable infection by engaging CD4 and a chemokine coreceptor, either CCR5 or CXCR4. The variable loop 3 (V3) of the HIV-1 envelope protein (Env) is the main determinant for coreceptor usage. The predominant CCR5 using (R5) HIV-1 Env has been intensively studied in function and structure, whereas the trimeric architecture of the less frequent, but more cytopathic CXCR4 using (X4) HIV-1 Env is largely unknown, as are the consequences of sequence changes in and near V3 on antigenicity and trimeric Env structure.
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Antigenic and 3D structural characterization of soluble X4 and hybrid X4-R5 HIV-1 Env trimers. 2014, 11:42 Retrovirology
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en
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1742-4690
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