Lack of interference between IgA-binding proteins and IgA proteases of human pathogenic bacteria
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1110281
- author
- Stenberg, Lars LU ; Qiu, J ; Lindahl, Gunnar LU and Plaut, A G
- organization
- publishing date
- 1996
- 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
- 2016-04-01 16:02:07
- date last changed
- 2022-01-28 08:49:48
@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}}, }