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Studies on the neutralization of herpes simplex virus. XI. Differences between slow-reacting complement-requiring neutralizing (s-CRN) antibodies in IgG and IgM.
Microbiol Immunol ; 24(11): 1069-77, 1980.
Article em En | MEDLINE | ID: mdl-6261091
ABSTRACT
Late IgG and IgM from a rabbit immunized with herpes virus were tested for ordinary neutralizing (N) antibody, complement-requiring neutralizing (CRN) antibody and in addition CRN antibody detectable by overnight sensitization at 0 C (s-CRN antibody). Heat stability tests showed that IgG s-CRN antibody was slightly less resistant to heating at 70 C than were N and CRN antibodies, whereas all three activities of IgM were quickly degraded at this temperature. Dose-response curves with varying amounts of complement (C) or anti-antibody revealed a marked difference between IgG s-CRN and IgM s-CRN antibodies. While 1-hr sensitization at 37 C was insufficient to detect IgG s-CRN antibody, it had the same effect as overnight sensitization at 0 C for IgM s-CRN antibody. When sensitization at 0 C was prolonged to 3 days, unexpectedly high endpoints exceeding 110,000 were obtained even with IgM. consequently, enhancement by C was several hundred-fold with IgM in contrast to 5- to 10-fold enhancement of IgG s-CRN antibody, which was similar to that after overnight sensitization. Also IgM obviously required more C than did IgG. These results suggest that IgM of late serum is slower reacting and more C-dependent than IgG s-CRN antibody. Tests with early rabbit sera indicated that the s-CRN antibody detectable by 3-day sensitization reaches a high level before the appearance of N antibody.
Assuntos
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Base de dados: MEDLINE Assunto principal: Imunoglobulina G / Imunoglobulina M / Simplexvirus / Anticorpos Antivirais Limite: Animals Idioma: En Ano de publicação: 1980 Tipo de documento: Article
Buscar no Google
Base de dados: MEDLINE Assunto principal: Imunoglobulina G / Imunoglobulina M / Simplexvirus / Anticorpos Antivirais Limite: Animals Idioma: En Ano de publicação: 1980 Tipo de documento: Article