Antigenic structure of human chorionic somatomammotropin: Four epitopes revealed by monoclonal antibodies

Mariani, Massimo A.; Cianfriglia, Maurizio; Neri, Paolo; Lafata, M.; Antoni, G.

doi:10.1016/0022-1759(84)90123-6

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Monoclonal Antibodies Epitopes and Cross-reactivity1

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1985

1992

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Cited by 5 publications

(1 citation statement)

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“…172 Fifteen monoclonal antibodies against hPL could be divided into four groups recognizing four different epitopes. 173 Two monoclonal antibodies prepared against sal mon GH were specific for this hormone and did not react with salmon PRL. On the other hand, another two monoclonal antibodies prepared against salmon PRL were specific.…”

Section: Monoclonal Antibodies Epitopes and Cross-reactivitymentioning

confidence: 99%

The Immunology of Prolactin

Berczi¹

1992

Semin Reprod Med

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Section: Monoclonal Antibodies Epitopes and Cross-reactivitymentioning

confidence: 99%

The Immunology of Prolactin

Berczi¹

1992

Semin Reprod Med

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Major antigenic domain recognized by monoclonal antibodies maps within the carboxy‐terminal moiety of a recombinant human immunodeficiency virus‐1 p24 protein

Gallina

Rossi

Mariani³

et al. 1990

Journal of Medical Virology

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Antigenicity in mice of a recombinant polypeptide including the complete amino acid sequence of mature human immunodeficiency virus type 1 p24 protein was studied by induction of monoclonal antibodies (MAbs). A panel of nine recloned hybridomas secreting MAbs with anti-p24 reactivity was isolated and further characterized. Competitive inhibition experiments suggested that the MAbs could be grouped into four epitopic classes corresponding to at least two distinct determinants. Analysis of reactivity to recombinant p24 deletion variants indicated that all the recognized epitopes are localized within a carboxy-terminal domain (amino acids 168-208) which should be largely exposed in recombinant as well as authentic antigen. Lack of response to N-terminal and central portions of p24 suggests that the antigenicity of those regions in the natural polypeptide is strongly conformation-dependent.

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