Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae, is a lipoprotein
(1992) In Infection and Immunity 60(4). p.1336-1342- Abstract
- Protein D is an immunoglobulin D-binding membrane protein exposed on the surface of the gram-negative bacterium Haemophilus influenzae. Results reported here indicate that protein D is a lipoprotein. The protein is apparently synthesized as a precursor with an 18-residue-long signal sequence modified by the covalent attachment of both ester-linked and amide-linked palmitate to the cysteine residue, which becomes the amino terminus after cleavage of the signal sequence. Globomycin inhibited maturation of protein D in H. influenzae, implying that protein D is exported through the lipoprotein export pathway. A mutant expressing a protein D lacking the cysteine residue was constructed by oligonucleotide site-directed mutagenesis. The mutated... (More)
- Protein D is an immunoglobulin D-binding membrane protein exposed on the surface of the gram-negative bacterium Haemophilus influenzae. Results reported here indicate that protein D is a lipoprotein. The protein is apparently synthesized as a precursor with an 18-residue-long signal sequence modified by the covalent attachment of both ester-linked and amide-linked palmitate to the cysteine residue, which becomes the amino terminus after cleavage of the signal sequence. Globomycin inhibited maturation of protein D in H. influenzae, implying that protein D is exported through the lipoprotein export pathway. A mutant expressing a protein D lacking the cysteine residue was constructed by oligonucleotide site-directed mutagenesis. The mutated protein D molecule was not acylated and partitioned in the aqueous phase after Triton X-114 extraction of intact bacteria, unlike native and recombinant protein D, which partitioned in the detergent phase. The nonacylated protein D molecule was localized to the periplasmic space of Escherichia coli. The hydrophilic protein D molecule will be used in investigations concerning its ability to function as a vaccine component. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1106384
- author
- Janson, Håkan LU ; Heden, L O and Forsgren, Arne LU
- organization
- publishing date
- 1992
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Infection and Immunity
- volume
- 60
- issue
- 4
- pages
- 1336 - 1342
- publisher
- American Society for Microbiology
- external identifiers
-
- pmid:1548059
- scopus:0026575959
- ISSN
- 1098-5522
- language
- English
- LU publication?
- yes
- id
- 02bb1877-ea9b-4dd3-9e35-103f12bd10b8 (old id 1106384)
- alternative location
- http://iai.asm.org/cgi/content/abstract/60/4/1336
- date added to LUP
- 2016-04-01 11:55:50
- date last changed
- 2021-01-03 04:30:31
@article{02bb1877-ea9b-4dd3-9e35-103f12bd10b8,
abstract = {{Protein D is an immunoglobulin D-binding membrane protein exposed on the surface of the gram-negative bacterium Haemophilus influenzae. Results reported here indicate that protein D is a lipoprotein. The protein is apparently synthesized as a precursor with an 18-residue-long signal sequence modified by the covalent attachment of both ester-linked and amide-linked palmitate to the cysteine residue, which becomes the amino terminus after cleavage of the signal sequence. Globomycin inhibited maturation of protein D in H. influenzae, implying that protein D is exported through the lipoprotein export pathway. A mutant expressing a protein D lacking the cysteine residue was constructed by oligonucleotide site-directed mutagenesis. The mutated protein D molecule was not acylated and partitioned in the aqueous phase after Triton X-114 extraction of intact bacteria, unlike native and recombinant protein D, which partitioned in the detergent phase. The nonacylated protein D molecule was localized to the periplasmic space of Escherichia coli. The hydrophilic protein D molecule will be used in investigations concerning its ability to function as a vaccine component.}},
author = {{Janson, Håkan and Heden, L O and Forsgren, Arne}},
issn = {{1098-5522}},
language = {{eng}},
number = {{4}},
pages = {{1336--1342}},
publisher = {{American Society for Microbiology}},
series = {{Infection and Immunity}},
title = {{Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae, is a lipoprotein}},
url = {{http://iai.asm.org/cgi/content/abstract/60/4/1336}},
volume = {{60}},
year = {{1992}},
}