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Lack of interference between IgA-binding proteins and IgA proteases of human pathogenic bacteria

Stenberg, Lars LU ; Qiu, J; Lindahl, Gunnar LU and Plaut, A G (1996) In Journal of Medical Microbiology 44(1). p.65-69
Abstract
Some human bacterial pathogens produce specific immunoglobulin A1 (IgA1) proteases that cleave the heavy chain of human IgA1, generating intact Fab and Fc fragments. Other pathogenic bacterial species express surface proteins which bind to the Fc part of human IgA in a non-immune manner. To analyse whether IgA-binding proteins affect the activity of IgA1 proteases, the ability of seven different IgA1 proteases to hydrolyse IgA1 in the presence of either of two different bacterial IgA-binding proteins was tested. Data obtained in two different types of experiment suggest that IgA1 bound to IgA-binding proteins still functions as a substrate for IgA1 proteases. As Fc fragments produced by cleaving IgA1 with IgA1 proteases still bind to... (More)
Some human bacterial pathogens produce specific immunoglobulin A1 (IgA1) proteases that cleave the heavy chain of human IgA1, generating intact Fab and Fc fragments. Other pathogenic bacterial species express surface proteins which bind to the Fc part of human IgA in a non-immune manner. To analyse whether IgA-binding proteins affect the activity of IgA1 proteases, the ability of seven different IgA1 proteases to hydrolyse IgA1 in the presence of either of two different bacterial IgA-binding proteins was tested. Data obtained in two different types of experiment suggest that IgA1 bound to IgA-binding proteins still functions as a substrate for IgA1 proteases. As Fc fragments produced by cleaving IgA1 with IgA1 proteases still bind to IgA-binding proteins, we conclude that these two types of bacterial protein act independently of each other. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Medical Microbiology
volume
44
issue
1
pages
65 - 69
publisher
Lippincott Williams & Wilkins
external identifiers
  • pmid:8544214
  • scopus:0030042912
ISSN
0022-2615
language
English
LU publication?
yes
id
e1236f09-64e4-438e-acd8-e399aecfa1ef (old id 1110281)
date added to LUP
2008-07-30 08:39:52
date last changed
2017-01-01 06:53:44
@article{e1236f09-64e4-438e-acd8-e399aecfa1ef,
  abstract     = {Some human bacterial pathogens produce specific immunoglobulin A1 (IgA1) proteases that cleave the heavy chain of human IgA1, generating intact Fab and Fc fragments. Other pathogenic bacterial species express surface proteins which bind to the Fc part of human IgA in a non-immune manner. To analyse whether IgA-binding proteins affect the activity of IgA1 proteases, the ability of seven different IgA1 proteases to hydrolyse IgA1 in the presence of either of two different bacterial IgA-binding proteins was tested. Data obtained in two different types of experiment suggest that IgA1 bound to IgA-binding proteins still functions as a substrate for IgA1 proteases. As Fc fragments produced by cleaving IgA1 with IgA1 proteases still bind to IgA-binding proteins, we conclude that these two types of bacterial protein act independently of each other.},
  author       = {Stenberg, Lars and Qiu, J and Lindahl, Gunnar and Plaut, A G},
  issn         = {0022-2615},
  language     = {eng},
  number       = {1},
  pages        = {65--69},
  publisher    = {Lippincott Williams & Wilkins},
  series       = {Journal of Medical Microbiology},
  title        = {Lack of interference between IgA-binding proteins and IgA proteases of human pathogenic bacteria},
  volume       = {44},
  year         = {1996},
}