Antibodies against synthetic peptides of herpes simplex virus type 1 glycoprotein D and their capability to neutralize viral infectivity in vitro.

Peptides corresponding to residues 1-13, 9-21, 18-30, 82-93, 137-150, 181-197, 232-243, 235-243, 267-281, 271-281 and 302-315 of glycoprotein D of herpes simplex virus type 1 (HSV-1) were chemically synthesized. These peptides were coupled to carrier proteins, and the resulting conjugates were used to immunize rabbits. An enzyme-linked immunosorbent assay was used to determine antipeptide antibody titers in serum collected after immunization.

Purification strategies for Sendai virus membrane proteins.

Viral membrane proteins extracted from Sendai virions with the non-ionic detergents decylpolyethyleneglycol-300 and Triton X-100 were used as a model mixture of hydrophobic membrane proteins. The detergent extract contained the fusion protein (F) and the tetrameric and dimeric forms of the hemagglutinin-neuraminidase protein (HN). These proteins were purified by size-exclusion high-performance liquid chromatography (HPLC) in the presence of 0.

Size-exclusion high-performance liquid chromatography of Sendai virus membrane proteins in different detergents. A comparison of different columns.

Four column packings for size-exclusion high-performance liquid chromatography (HPLC) of proteins with particle sizes from 3 to 13 micron were compared, using 0.1% sodium dodecyl sulphate in the solvent. Their suitability for the purification of hydrophobic membrane proteins was studied with Sendai virus proteins as a model.

Combined size-exclusion and reversed-phase high-performance liquid chromatography of a detergent extract of Sendai virus.

Virus envelope proteins obtained by Triton X-100 extraction of Sendai virions were purified to a high degree by a combination of high-performance liquid chromatography (HPLC) methods. Size-exclusion HPLC on a TSK 4000 PW column with several concentrations of acetonitrile or ethanol-1-butanol in 0.1% hydrochloric acid as eluent was used as the first chromatographic step.