The gene encoding protein D (hpd) is highly conserved among Haemophilus influenzae type b and nontypeable strains
(1995) In Infection and Immunity 63(2). p.696-699- Abstract
- The molecular conservation of a surface-exposed lipoprotein, protein D, of Haemophilus influenzae was studied by cloning and sequencing of the gene encoding protein D from three encapsulated type b strains and three nontypeable strains of H. influenzae. These nucleotide sequences were analyzed with previously reported sequences from one type b strain and one nontypeable strain. The nucleotide sequences and the deduced amino acid sequences for protein D were highly conserved. The deduced amino acid sequence (364 amino acids) of protein D from six strains differed only in two amino acids near the C-terminal end. The remaining two strains, one type b and one nontypeable, differed from the consensus sequence in 7 amino acids each. Protein D is... (More)
- The molecular conservation of a surface-exposed lipoprotein, protein D, of Haemophilus influenzae was studied by cloning and sequencing of the gene encoding protein D from three encapsulated type b strains and three nontypeable strains of H. influenzae. These nucleotide sequences were analyzed with previously reported sequences from one type b strain and one nontypeable strain. The nucleotide sequences and the deduced amino acid sequences for protein D were highly conserved. The deduced amino acid sequence (364 amino acids) of protein D from six strains differed only in two amino acids near the C-terminal end. The remaining two strains, one type b and one nontypeable, differed from the consensus sequence in 7 amino acids each. Protein D is 64 and 36% identical and 77 and 56% similar to the glycerophosphodiester phosphodiesterases (GlpQ) of Escherichia coli and Bacillus subtilis. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1109019
- author
- Song, Xin-Ming ; Forsgren, Arne LU and Janson, Håkan LU
- organization
- publishing date
- 1995
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Infection and Immunity
- volume
- 63
- issue
- 2
- pages
- 696 - 699
- publisher
- American Society for Microbiology
- external identifiers
-
- pmid:7822043
- scopus:0028942233
- ISSN
- 1098-5522
- language
- English
- LU publication?
- yes
- id
- 4626e675-fa7c-4623-bce4-3e2f76435647 (old id 1109019)
- alternative location
- http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=173053
- date added to LUP
- 2016-04-01 12:18:30
- date last changed
- 2021-08-22 04:51:43
@article{4626e675-fa7c-4623-bce4-3e2f76435647,
abstract = {{The molecular conservation of a surface-exposed lipoprotein, protein D, of Haemophilus influenzae was studied by cloning and sequencing of the gene encoding protein D from three encapsulated type b strains and three nontypeable strains of H. influenzae. These nucleotide sequences were analyzed with previously reported sequences from one type b strain and one nontypeable strain. The nucleotide sequences and the deduced amino acid sequences for protein D were highly conserved. The deduced amino acid sequence (364 amino acids) of protein D from six strains differed only in two amino acids near the C-terminal end. The remaining two strains, one type b and one nontypeable, differed from the consensus sequence in 7 amino acids each. Protein D is 64 and 36% identical and 77 and 56% similar to the glycerophosphodiester phosphodiesterases (GlpQ) of Escherichia coli and Bacillus subtilis.}},
author = {{Song, Xin-Ming and Forsgren, Arne and Janson, Håkan}},
issn = {{1098-5522}},
language = {{eng}},
number = {{2}},
pages = {{696--699}},
publisher = {{American Society for Microbiology}},
series = {{Infection and Immunity}},
title = {{The gene encoding protein D (hpd) is highly conserved among Haemophilus influenzae type b and nontypeable strains}},
url = {{http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=173053}},
volume = {{63}},
year = {{1995}},
}