Protein D of Haemophilus influenzae. A novel bacterial surface protein with affinity for human IgD
(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
- Ruan, Maorong ; Akkoyunlu, Mustafa LU ; Grubb, A LU and Forsgren, A LU
- organization
- publishing date
- 1990
- 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
-
- scopus:0025204727
- pmid:2230124
- 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
- 2024-01-12 02:54:47
@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}}, }