Advanced

Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae, is a lipoprotein

Janson, Håkan LU ; Heden, L O and Forsgren, Arne LU (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:
author
organization
publishing date
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
2008-08-01 16:45:13
date last changed
2017-07-30 03:38:51
@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},
  volume       = {60},
  year         = {1992},
}