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Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D.

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Academic year: 2019

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Figure

FIG. 1. Schematic representations of full-length and truncated HSV gD. (A)Full-length gD expressed on HSV virion and infected cell surfaces
FIG. 2. SDS-PAGE analysis of gD-1 mutants. Purified proteins were elec-trophoresed under denaturing conditions on 10% polyacrylamide gels and either
TABLE 2. Secondary-structure content of gDta
FIG. 4. Effect of temperature on antigenic conformation of gDt. Proteins were heated for 5 min at temperatures ranging from 37 to 100�coat 96-well plates, and subjected to ELISA with MAb HD1, which recognizes a discontinuous epitope (A), or MAb DL6, which
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