Binding of Secretory Component to Dimers of Immunoglobulin A in vitro. A Model for the Interactions of the Two Moieties in Secretory Immunoglobulin A

1974 ◽  
Vol 45 (1) ◽  
pp. 261-268 ◽  
Author(s):  
Erik Lindh ◽  
Ingemar Bjork
Keyword(s):  
Immunoglobulin A ◽  
Secretory Component ◽  
Secretory Immunoglobulin A ◽  
Secretory Immunoglobulin

scholarly journals Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin

2020 ◽  
Author(s):  
Yuxin Wang ◽  
Guopeng Wang ◽  
Yaxin Li ◽  
Hao Shen ◽  
Huarui Chu ◽  
...  
Keyword(s):  
Specific Interaction ◽  
Immunoglobulin A ◽  
Underlying Mechanism ◽  
Secretory Component ◽  
Secretory Immunoglobulin A ◽  
Immunoglobulin Receptor ◽  
J Chain ◽  
Cryo Electron Microscopy ◽  
Structural Insights ◽  
Secretory Immunoglobulin

AbstractSecretory Immunoglobulin A (SIgA) is the most abundant antibody at the mucosal surface. SIgA possesses two additional subunits besides IgA: the joining chain (J-chain) and secretory component (SC). SC is the ectodomain of the polymeric immunoglobulin receptor (pIgR), which functions to transport IgA to the mucosa. The underlying mechanism of how the J-chain and pIgR/SC facilitates the assembly and secretion of SIgA remains to be understood. During the infection of Streptococcus pneumoniae, a pneumococcal adhesin SpsA hijacks SIgA and unliganded pIgR/SC to evade host defense and gain entry to human cells. How SpsA specifically targets SIgA and pIgR/SC also remains unclear. Here we report a cryo-electron microscopy structure of the Fc region of human IgA1 (Fcα) in complex with J-chain and SC (Fcα-J-SC), which reveals the organization principle of SIgA. We also present the structure of Fcα-J-SC in complex with SpsA, which uncovers the specific interaction between SpsA and human pIgR/SC. These results advance the molecular understanding of SIgA and shed light on the pathogenesis of S. pneumoniae.

Column enzyme immunoassay for secretory immunoglobulin A in serum.

1983 ◽  
Vol 29 (1) ◽  
pp. 151-153 ◽  
Author(s):  
R Yamamoto ◽  
S Kimura ◽  
S Hattori ◽  
Y Ishiguro ◽  
K Kato
Keyword(s):  
Enzyme Immunoassay ◽  
Sodium Carbonate Solution ◽  
Solid Phase ◽  
Immunoglobulin A ◽  
Enzyme Reaction ◽  
Secretory Component ◽  
Secretory Immunoglobulin A ◽  
Serum Samples ◽  
Sepharose 4B ◽  
Secretory Immunoglobulin

Abstract This enzyme immunoassay for specific measurement of secretory immunoglobulin A concentrations in human serum involves use of a small chromatographic column as a solid-phase. Serum samples are incubated for 2 h with beta-D-galactosidase-labeled antibody to secretory component, then passed through a 0.1-mL Sepharose 4B column containing antibodies to human immunoglobulin A. After the column is washed to remove the unbound label, the buffer in the column is replaced by a solution of o-nitrophenyl-beta-D-galactoside (a beta-D-galactosidase substrate) and incubated at 25 degrees C overnight. The enzyme reaction is stopped by washing the column with sodium carbonate solution, and the absorbance of the eluate is measured at 420 nm. The concentration of secretory immunoglobulin A can be determined with a minimum detectable sensitivity of 3 mg/L, without interference from free immunoglobulin A and secretory component in the same samples.

A comparative study of secretory immunoglobulin A and immunoglobulin G in host defense in an in vitro pneumonia model

2006 ◽  
Vol 191 (3) ◽  
pp. 386-390 ◽  
Author(s):  
Lawrence N. Diebel ◽  
David M. Liberati ◽  
Michael T. White ◽  
Clement A. Diglio ◽  
William J. Brown
Keyword(s):  
Comparative Study ◽  
Host Defense ◽  
Immunoglobulin G ◽  
Immunoglobulin A ◽  
Secretory Immunoglobulin A ◽  
Secretory Immunoglobulin

Interaction of secretory immunoglobulin A antibodies withNaegleria fowleritrophozoites and collagen type I

2003 ◽  
Vol 49 (3) ◽  
pp. 164-170 ◽  
Author(s):  
Mineko Shibayama ◽  
José de Jesús Serrano-Luna ◽  
Saúl Rojas-Hernández ◽  
Rafael Campos-Rodríguez ◽  
Víctor Tsutsumi
Keyword(s):  
Collagen Type ◽  
Immunoglobulin A ◽  
Collagen Type I ◽  
Secretory Iga ◽  
Type I ◽  
Secretory Immunoglobulin A ◽  
Naegleria Fowleri ◽  
Nægleria Fowleri ◽  
Secretory Immunoglobulin

In this work, we analyzed the in vitro interaction of human secretory immunoglobulin A (sIgA) antibodies with Naegleria fowleri trophozoites and the capacity of these antibodies to inhibit amoeba adherence to collagen type I. We also studied N. fowleri antigens that are recognized by sIgA, using immunoblot assays. Immunocytochemical analysis of the interaction showed a redistribution of antigens on the surface of trophozoites by sIgA antibodies. Ultrastructural analysis of antibody–amoeba interaction showed that besides the patching and cap formation, parasites were capable of eliminating the antigen–antibody complex produced on the surface. sIgA antibodies were capable of inhibiting the in vitro adhesion of trophozoites to collagen type I. We suggest that nonsymptomatic infections by N. fowleri may stimulate a local specific immunity that prevents trophozoite adhesion and invasion of nasal mucosa.Key words: Naegleria fowleri, free-living amoebae, human antibodies, secretory IgA, mucosal immunity.

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