Difference between revisions of "Lentivirus internal"

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==Lentiviruses stepping inward==
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Proceeding inward, the viral matrix protein forms a layer just under the lipid bilayer.  The structure of this layer has been controversial.  Figure 1 shows one proposal, hexagonal packing of MA trimers (yellow)(Alfadhli et al. 2009).  Movie 2 shows an MA hexamer bound to a modeled membrane.
 
Proceeding inward, the viral matrix protein forms a layer just under the lipid bilayer.  The structure of this layer has been controversial.  Figure 1 shows one proposal, hexagonal packing of MA trimers (yellow)(Alfadhli et al. 2009).  Movie 2 shows an MA hexamer bound to a modeled membrane.
 
Lentivirus particles are distinguished by the presence of a bullet-shaped capsid (orange) assembled from monomers of the viral capsid protein (CA).  The cone is a hollow "fullerene cone" built up from CA hexamers (Movie 3) assembled together with twelve CA pentamers (Ganser et al. 1999).
 
Lentivirus particles are distinguished by the presence of a bullet-shaped capsid (orange) assembled from monomers of the viral capsid protein (CA).  The cone is a hollow "fullerene cone" built up from CA hexamers (Movie 3) assembled together with twelve CA pentamers (Ganser et al. 1999).

Revision as of 16:55, 23 September 2011

« The HIV replication cycle: a web-based interactive account

Lentiviruses Internally

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Lentiviruses Externally Lentiviral Capsid

Lentiviruses stepping inward

Proceeding inward, the viral matrix protein forms a layer just under the lipid bilayer. The structure of this layer has been controversial. Figure 1 shows one proposal, hexagonal packing of MA trimers (yellow)(Alfadhli et al. 2009). Movie 2 shows an MA hexamer bound to a modeled membrane. Lentivirus particles are distinguished by the presence of a bullet-shaped capsid (orange) assembled from monomers of the viral capsid protein (CA). The cone is a hollow "fullerene cone" built up from CA hexamers (Movie 3) assembled together with twelve CA pentamers (Ganser et al. 1999).