Biology Reference
In-Depth Information
WT
C175S
C185S
C428S
Fig. 2.
Electron micrographs of particles formed by HPV16 L1 (WT),
C175S (the HPV16 L1 mutant with substitution of S for C at amino acid
175), C185S, and C428S.
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The particles are obtained by expression of the
L1 genes with or without mutations in insect sf9 cells from recombinant
baculoviruses.
may be necessary to form an icosahedral structure composed of pen-
tavalent and hexavalent capsomeres.
The locations of cysteines are well-conserved in the L1 proteins from
various HPVs. The importance of C175 and C428 in HPV16 L1 is con-
sistent with the results of the studies of cysteine mutants of HPV33.
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