IgG antibodies to secretory component in normal human serum

J. B. Splawski, C. S. Woodard, R. M. Denney, R. M. Goldblum

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

While isolating free secretory component (FSC) by monoclonal antibody affinity chromatography, we demonstrated FSC-IgG complexes in human milk. We hypothesized that IgG antibody to secretory component (SC) might be transported into the milk from the serum. We therefore examined sera from 10 normal adults and 10 infants for IgG capable of binding to FSC in an enzyme-linked immunosorbent assay. Eight of 10 normal adult sera and nine of 10 infant sera demonstrated IgG binding to FSC with titers ranging from 1:54 to 1:4096. Quantitation of the IgG bound to FSC was hampered in adult sera by the binding of IgM and polymeric IgA to the FSC. Quantitation in five infant sera ranged from 0.5 to 6.4 μg/ml. A pepsin digest of an IgG fraction of serum demonstrated binding of the F(ab')2 fragments to the FSC. The specificity of the antibodies in human serum was evaluated by examining the binding to secretory IgA (sIgA) and FSC isolated from pooled human milk and polymeric IgA isolated from the ascitic fluid of a patient with an IgA myeloma. Eight of the 10 adults had antibody specific for FSC. Three of the eight, all female, also had antibody specific for sIgA. Two of the eight had antibody either to FSC and sIgA or to FSC plus an antibody that could bind to an epitope shared by sIgA and FSC. Competition experiments with monoclonal antibodies to human secretory component and sIgA were used to confirm and further define these specificities. The results of this study indicate that antibody to SC is common in normal adult and infant sera. The majority of antibodies seem to be directed against epitopes present on FSC but not on sIgA, which suggests sensitization to circulating or membrane-bound SC. The significance of these antibodies in normal human sera remains to be elucidated.

Original languageEnglish (US)
Pages (from-to)2111-2115
Number of pages5
JournalJournal of Immunology
Volume133
Issue number4
StatePublished - 1984

Fingerprint

Secretory Component
Immunoglobulin G
Antibodies
Serum
Secretory Immunoglobulin A
Human Milk
Epitopes
Monoclonal Antibodies
Antibody Affinity
Antibody Specificity

ASJC Scopus subject areas

  • Immunology

Cite this

Splawski, J. B., Woodard, C. S., Denney, R. M., & Goldblum, R. M. (1984). IgG antibodies to secretory component in normal human serum. Journal of Immunology, 133(4), 2111-2115.

IgG antibodies to secretory component in normal human serum. / Splawski, J. B.; Woodard, C. S.; Denney, R. M.; Goldblum, R. M.

In: Journal of Immunology, Vol. 133, No. 4, 1984, p. 2111-2115.

Research output: Contribution to journalArticle

Splawski, JB, Woodard, CS, Denney, RM & Goldblum, RM 1984, 'IgG antibodies to secretory component in normal human serum', Journal of Immunology, vol. 133, no. 4, pp. 2111-2115.
Splawski JB, Woodard CS, Denney RM, Goldblum RM. IgG antibodies to secretory component in normal human serum. Journal of Immunology. 1984;133(4):2111-2115.
Splawski, J. B. ; Woodard, C. S. ; Denney, R. M. ; Goldblum, R. M. / IgG antibodies to secretory component in normal human serum. In: Journal of Immunology. 1984 ; Vol. 133, No. 4. pp. 2111-2115.
@article{3c3a8daed4a34245bad4c93608734748,
title = "IgG antibodies to secretory component in normal human serum",
abstract = "While isolating free secretory component (FSC) by monoclonal antibody affinity chromatography, we demonstrated FSC-IgG complexes in human milk. We hypothesized that IgG antibody to secretory component (SC) might be transported into the milk from the serum. We therefore examined sera from 10 normal adults and 10 infants for IgG capable of binding to FSC in an enzyme-linked immunosorbent assay. Eight of 10 normal adult sera and nine of 10 infant sera demonstrated IgG binding to FSC with titers ranging from 1:54 to 1:4096. Quantitation of the IgG bound to FSC was hampered in adult sera by the binding of IgM and polymeric IgA to the FSC. Quantitation in five infant sera ranged from 0.5 to 6.4 μg/ml. A pepsin digest of an IgG fraction of serum demonstrated binding of the F(ab')2 fragments to the FSC. The specificity of the antibodies in human serum was evaluated by examining the binding to secretory IgA (sIgA) and FSC isolated from pooled human milk and polymeric IgA isolated from the ascitic fluid of a patient with an IgA myeloma. Eight of the 10 adults had antibody specific for FSC. Three of the eight, all female, also had antibody specific for sIgA. Two of the eight had antibody either to FSC and sIgA or to FSC plus an antibody that could bind to an epitope shared by sIgA and FSC. Competition experiments with monoclonal antibodies to human secretory component and sIgA were used to confirm and further define these specificities. The results of this study indicate that antibody to SC is common in normal adult and infant sera. The majority of antibodies seem to be directed against epitopes present on FSC but not on sIgA, which suggests sensitization to circulating or membrane-bound SC. The significance of these antibodies in normal human sera remains to be elucidated.",
author = "Splawski, {J. B.} and Woodard, {C. S.} and Denney, {R. M.} and Goldblum, {R. M.}",
year = "1984",
language = "English (US)",
volume = "133",
pages = "2111--2115",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "4",

}

TY - JOUR

T1 - IgG antibodies to secretory component in normal human serum

AU - Splawski, J. B.

AU - Woodard, C. S.

AU - Denney, R. M.

AU - Goldblum, R. M.

PY - 1984

Y1 - 1984

N2 - While isolating free secretory component (FSC) by monoclonal antibody affinity chromatography, we demonstrated FSC-IgG complexes in human milk. We hypothesized that IgG antibody to secretory component (SC) might be transported into the milk from the serum. We therefore examined sera from 10 normal adults and 10 infants for IgG capable of binding to FSC in an enzyme-linked immunosorbent assay. Eight of 10 normal adult sera and nine of 10 infant sera demonstrated IgG binding to FSC with titers ranging from 1:54 to 1:4096. Quantitation of the IgG bound to FSC was hampered in adult sera by the binding of IgM and polymeric IgA to the FSC. Quantitation in five infant sera ranged from 0.5 to 6.4 μg/ml. A pepsin digest of an IgG fraction of serum demonstrated binding of the F(ab')2 fragments to the FSC. The specificity of the antibodies in human serum was evaluated by examining the binding to secretory IgA (sIgA) and FSC isolated from pooled human milk and polymeric IgA isolated from the ascitic fluid of a patient with an IgA myeloma. Eight of the 10 adults had antibody specific for FSC. Three of the eight, all female, also had antibody specific for sIgA. Two of the eight had antibody either to FSC and sIgA or to FSC plus an antibody that could bind to an epitope shared by sIgA and FSC. Competition experiments with monoclonal antibodies to human secretory component and sIgA were used to confirm and further define these specificities. The results of this study indicate that antibody to SC is common in normal adult and infant sera. The majority of antibodies seem to be directed against epitopes present on FSC but not on sIgA, which suggests sensitization to circulating or membrane-bound SC. The significance of these antibodies in normal human sera remains to be elucidated.

AB - While isolating free secretory component (FSC) by monoclonal antibody affinity chromatography, we demonstrated FSC-IgG complexes in human milk. We hypothesized that IgG antibody to secretory component (SC) might be transported into the milk from the serum. We therefore examined sera from 10 normal adults and 10 infants for IgG capable of binding to FSC in an enzyme-linked immunosorbent assay. Eight of 10 normal adult sera and nine of 10 infant sera demonstrated IgG binding to FSC with titers ranging from 1:54 to 1:4096. Quantitation of the IgG bound to FSC was hampered in adult sera by the binding of IgM and polymeric IgA to the FSC. Quantitation in five infant sera ranged from 0.5 to 6.4 μg/ml. A pepsin digest of an IgG fraction of serum demonstrated binding of the F(ab')2 fragments to the FSC. The specificity of the antibodies in human serum was evaluated by examining the binding to secretory IgA (sIgA) and FSC isolated from pooled human milk and polymeric IgA isolated from the ascitic fluid of a patient with an IgA myeloma. Eight of the 10 adults had antibody specific for FSC. Three of the eight, all female, also had antibody specific for sIgA. Two of the eight had antibody either to FSC and sIgA or to FSC plus an antibody that could bind to an epitope shared by sIgA and FSC. Competition experiments with monoclonal antibodies to human secretory component and sIgA were used to confirm and further define these specificities. The results of this study indicate that antibody to SC is common in normal adult and infant sera. The majority of antibodies seem to be directed against epitopes present on FSC but not on sIgA, which suggests sensitization to circulating or membrane-bound SC. The significance of these antibodies in normal human sera remains to be elucidated.

UR - http://www.scopus.com/inward/record.url?scp=0021224664&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021224664&partnerID=8YFLogxK

M3 - Article

C2 - 6332148

AN - SCOPUS:0021224664

VL - 133

SP - 2111

EP - 2115

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 4

ER -