Abstract
Antigens detected by the complement-fixation (CF) test were prepared from BHK-21 cells infected with Pichinde virus. The preparations contained two antigens demonstrable by immunodiffusion. The antigen present in abundance was heat stable, Pronase resistant, and had a molecular weight of 20,000 to 30,000 as estimated by gel filtration. Polyacrylamide gel electrophoresis of purified antigen demonstrated two low-molecular-weight polypeptides. An identical antigenic determinant was found by disrupting purified virus with Nonidet P-40; however, none of the viral polypeptides co-migrated with the polypeptides derived from purified CF antigen. Pronase digestion of disrupted virus did not alter antigenicity but degraded the viral peptides to sizes similar to those associated with the major CF antigen. These observations suggest that the major CF antigen of Pichnide virus is a cleavage product of the structural proteins of the virus.
MeSH Terms
Antigens, Viral/analysis
Arenaviruses, New World/analysis,immunology
Cell Line
Complement Fixation Tests
Epitopes
Molecular Weight
Peptides/analysis
RNA Viruses/immunology
Solubility
Viral Proteins/analysis,immunology
Chemicals
Antigens, Viral
Epitopes
Peptides
Viral Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Buchmeier M J
Gee S R
Rawls W E
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