TABLE 3.

Assembly characteristics of the HPV-16 L1ΔN10 and L1ΔN10dCys capsomeresa

Capsomere constructAssembly procedureResulting assembly structurec
Dialysis/dilutionBufferTemp (°C)b
L1ΔN10DialysisAssembly bufferRTSmall VLPs (Ø, 35-40 nm)
DialysisPBSRTSmall VLPs (Ø, 35-40 nm)
DialysisVLP bufferRTSmall VLPs (Ø, 35-40 nm)
DialysisPBS37Small VLPs (Ø, 35-40 nm) and capsomeres
DilutionAssembly bufferRTSmall VLPs (Ø, 35-40 nm)
DilutionPBSRTSmall VLPs (Ø, 30 nm) and capsomeres
DilutionPBS37Small VLPs (Ø, 30 nm) and capsomeres
L1ΔN10dCysDialysisAssembly bufferRTSmall VLPs, aggregates (?)
DialysisPBSRTSmall VLPs, aggregates (?)
DialysisPBS37Capsomeres
DilutionPBSRTSmall VLPs, aggregates (?)
DilutionPBS37Capsomeres
  • a The L1ΔN10 and L1ΔN10dCys proteins were dialyzed against or diluted in PBS, VLP buffer, or assembly buffer at room temperature or 37°C. The resulting assembly forms were characterized by electron microscopy and sedimentation analysis and subsequent ELISA and Western blot analysis of the sucrose gradient fractions. Results of the analyses are given in the Resulting assembly structure column.

  • b RT, room temperature.

  • c The diameter of the particles (Ø) is given in parentheses. Aggregates were not clearly definable by electron microscopic analysis, which is indicated by a question mark in parentheses.