Protein D, the glycerophosphodiester phosphodiesterase from Haemophilus influenzae with affinity for human immunoglobulin D, influences virulence in a rat otitis model
(1994) In Infection and Immunity 62(11). p.4848-4854- Abstract
- A mutant lacking the ability to express the surface-exposed lipoprotein protein D was constructed by linker insertion and deletion mutagenesis of a cloned DNA insert containing the protein D structural gene from a nontypeable Haemophilus influenzae strain (NTHi). An isogenic NTHi mutant was isolated after transformation of genetically competent bacteria. The transformant was unreactive to a protein D-specific monoclonal antibody in a colony immunoassay. In addition, the mutant lacked the ability to synthesize detectable levels of protein D by protein staining, immunoblot methods, glycerophosphodiester phosphodiesterase activity, and binding studies of radiolabelled immunoglobulin D. The isogenic protein D-deficient mutant was compared with... (More)
- A mutant lacking the ability to express the surface-exposed lipoprotein protein D was constructed by linker insertion and deletion mutagenesis of a cloned DNA insert containing the protein D structural gene from a nontypeable Haemophilus influenzae strain (NTHi). An isogenic NTHi mutant was isolated after transformation of genetically competent bacteria. The transformant was unreactive to a protein D-specific monoclonal antibody in a colony immunoassay. In addition, the mutant lacked the ability to synthesize detectable levels of protein D by protein staining, immunoblot methods, glycerophosphodiester phosphodiesterase activity, and binding studies of radiolabelled immunoglobulin D. The isogenic protein D-deficient mutant was compared with its parental strain for its ability to induce experimental otitis media in rats challenged with bacteria. An approximately 100-times-higher concentration of the mutant compared with that of the wild-type strain was required in order to cause otitis among all rats challenged with that given dose. The protein D mutant exhibited a generation time that was equal to that of the wild-type strain in complex broth medium. No difference in lipopolysaccharide expression was found between the mutant and the parental strain. These results suggest that protein D may influence the pathogenesis of NTHi in the upper respiratory tract. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1107890
- author
- Janson, Håkan LU ; Melhus, Åsa LU ; Hermansson, Ann LU and Forsgren, Arne LU
- organization
- publishing date
- 1994
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Infection and Immunity
- volume
- 62
- issue
- 11
- pages
- 4848 - 4854
- publisher
- American Society for Microbiology
- external identifiers
-
- pmid:7927765
- scopus:0028029782
- ISSN
- 1098-5522
- language
- English
- LU publication?
- yes
- id
- 8364e6de-d6c7-42fd-96b5-0378e3e3ed35 (old id 1107890)
- alternative location
- http://iai.asm.org/cgi/reprint/62/11/4848
- date added to LUP
- 2016-04-01 12:36:27
- date last changed
- 2021-01-03 07:44:33
@article{8364e6de-d6c7-42fd-96b5-0378e3e3ed35, abstract = {{A mutant lacking the ability to express the surface-exposed lipoprotein protein D was constructed by linker insertion and deletion mutagenesis of a cloned DNA insert containing the protein D structural gene from a nontypeable Haemophilus influenzae strain (NTHi). An isogenic NTHi mutant was isolated after transformation of genetically competent bacteria. The transformant was unreactive to a protein D-specific monoclonal antibody in a colony immunoassay. In addition, the mutant lacked the ability to synthesize detectable levels of protein D by protein staining, immunoblot methods, glycerophosphodiester phosphodiesterase activity, and binding studies of radiolabelled immunoglobulin D. The isogenic protein D-deficient mutant was compared with its parental strain for its ability to induce experimental otitis media in rats challenged with bacteria. An approximately 100-times-higher concentration of the mutant compared with that of the wild-type strain was required in order to cause otitis among all rats challenged with that given dose. The protein D mutant exhibited a generation time that was equal to that of the wild-type strain in complex broth medium. No difference in lipopolysaccharide expression was found between the mutant and the parental strain. These results suggest that protein D may influence the pathogenesis of NTHi in the upper respiratory tract.}}, author = {{Janson, Håkan and Melhus, Åsa and Hermansson, Ann and Forsgren, Arne}}, issn = {{1098-5522}}, language = {{eng}}, number = {{11}}, pages = {{4848--4854}}, publisher = {{American Society for Microbiology}}, series = {{Infection and Immunity}}, title = {{Protein D, the glycerophosphodiester phosphodiesterase from Haemophilus influenzae with affinity for human immunoglobulin D, influences virulence in a rat otitis model}}, url = {{http://iai.asm.org/cgi/reprint/62/11/4848}}, volume = {{62}}, year = {{1994}}, }