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Protein D of Haemophilus influenzae. A novel bacterial surface protein with affinity for human IgD

Ruan, Maorong ; Akkoyunlu, Mustafa LU ; Grubb, A LU orcid and Forsgren, A LU (1990) In Journal of immunology 145(10). p.3379-3384
Abstract

Protein D, a novel surface protein of the bacterial species Haemophilus influenzae with affinity for human IgD, was isolated after solubilization with sonication and Sarcosyl-extraction by a single SDS-PAGE step. From 1 ml of packed bacteria was prepared 0.25 mg of purified protein D. The apparent m.w. of protein D was estimated to 42,000 by SDS-PAGE and gel chromatography. Edman degradation cycles of protein D produced no amino acid phenylthiohydantoin derivatives and the amino-terminal end of the single protein D polypeptide chain is thus probably blocked. Protein D differs from all previously described outer membrane proteins (protein 1 to 6) of H. influenzae. Thus, protein D did not react with antibodies against protein 1 or protein... (More)

Protein D, a novel surface protein of the bacterial species Haemophilus influenzae with affinity for human IgD, was isolated after solubilization with sonication and Sarcosyl-extraction by a single SDS-PAGE step. From 1 ml of packed bacteria was prepared 0.25 mg of purified protein D. The apparent m.w. of protein D was estimated to 42,000 by SDS-PAGE and gel chromatography. Edman degradation cycles of protein D produced no amino acid phenylthiohydantoin derivatives and the amino-terminal end of the single protein D polypeptide chain is thus probably blocked. Protein D differs from all previously described outer membrane proteins (protein 1 to 6) of H. influenzae. Thus, protein D did not react with antibodies against protein 1 or protein 2 and the latter proteins did not bind IgD. Protein D was found to exhibit unique Ig-binding properties. Thus, in dot blots protein D bound four different human IgD myeloma proteins but not IgG, IgM, IgA, IgE, or some additional proteins. On the IgD molecule, constant parts of the H chains both in the Fab and Fc fragments appear responsible for the interaction with protein D. This novel Ig-binding reagent promises to be of theoretical and practical interest in immunologic and microbiologic research.

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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Amino Acid Sequence, Bacterial Outer Membrane Proteins/isolation & purification, Carrier Proteins/isolation & purification, Haemophilus influenzae/analysis, Humans, Immunoglobulin D/metabolism, Molecular Weight
in
Journal of immunology
volume
145
issue
10
pages
3379 - 3384
publisher
American Association of Immunologists
external identifiers
  • pmid:2230124
  • scopus:0025204727
ISSN
0022-1767
language
English
LU publication?
yes
id
6abb5742-8a13-40d8-91d6-67313b2a5fdc
alternative location
https://www.jimmunol.org/content/145/10/3379.short
date added to LUP
2021-10-27 13:35:42
date last changed
2025-10-14 10:16:28
@article{6abb5742-8a13-40d8-91d6-67313b2a5fdc,
  abstract     = {{<p>Protein D, a novel surface protein of the bacterial species Haemophilus influenzae with affinity for human IgD, was isolated after solubilization with sonication and Sarcosyl-extraction by a single SDS-PAGE step. From 1 ml of packed bacteria was prepared 0.25 mg of purified protein D. The apparent m.w. of protein D was estimated to 42,000 by SDS-PAGE and gel chromatography. Edman degradation cycles of protein D produced no amino acid phenylthiohydantoin derivatives and the amino-terminal end of the single protein D polypeptide chain is thus probably blocked. Protein D differs from all previously described outer membrane proteins (protein 1 to 6) of H. influenzae. Thus, protein D did not react with antibodies against protein 1 or protein 2 and the latter proteins did not bind IgD. Protein D was found to exhibit unique Ig-binding properties. Thus, in dot blots protein D bound four different human IgD myeloma proteins but not IgG, IgM, IgA, IgE, or some additional proteins. On the IgD molecule, constant parts of the H chains both in the Fab and Fc fragments appear responsible for the interaction with protein D. This novel Ig-binding reagent promises to be of theoretical and practical interest in immunologic and microbiologic research.</p>}},
  author       = {{Ruan, Maorong and Akkoyunlu, Mustafa and Grubb, A and Forsgren, A}},
  issn         = {{0022-1767}},
  keywords     = {{Amino Acid Sequence; Bacterial Outer Membrane Proteins/isolation & purification; Carrier Proteins/isolation & purification; Haemophilus influenzae/analysis; Humans; Immunoglobulin D/metabolism; Molecular Weight}},
  language     = {{eng}},
  number       = {{10}},
  pages        = {{3379--3384}},
  publisher    = {{American Association of Immunologists}},
  series       = {{Journal of immunology}},
  title        = {{Protein D of Haemophilus influenzae. A novel bacterial surface protein with affinity for human IgD}},
  url          = {{https://www.jimmunol.org/content/145/10/3379.short}},
  volume       = {{145}},
  year         = {{1990}},
}