Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae

Research output: Contribution to journal › Article › peer-review

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Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae. / Boulnois, G J; Paton, J C; Mitchell, T J; Andrew, P W.

In: Molecular Microbiology, Vol. 5, No. 11, 11.1991, p. 2611-6.

Research output: Contribution to journal › Article › peer-review

Harvard

Boulnois, GJ, Paton, JC, Mitchell, TJ & Andrew, PW 1991, 'Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae', Molecular Microbiology, vol. 5, no. 11, pp. 2611-6.

APA

Boulnois, G. J., Paton, J. C., Mitchell, T. J., & Andrew, P. W. (1991). Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae. Molecular Microbiology, 5(11), 2611-6.

Vancouver

Boulnois GJ, Paton JC, Mitchell TJ, Andrew PW. Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae. Molecular Microbiology. 1991 Nov;5(11):2611-6.

Author

Boulnois, G J ; Paton, J C ; Mitchell, T J ; Andrew, P W. / Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae. In: Molecular Microbiology. 1991 ; Vol. 5, No. 11. pp. 2611-6.

Bibtex

@article{17756e65e33548efa4fe2a7eecfb6f82,
title = "Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae",
abstract = "Pneumolysin is a thiol-activated, membrane-damaging, multifunctional toxin and a known virulence factor of Streptococcus pneumoniae. The toxin can interfere with the functioning of both cellular and soluble components of the human immune system which protects against pneumococcal infection. Different amino acids within the toxin which are important in promoting oligomerization of the toxin in membranes and for the generation of functional lesions have been identified by site-directed mutagenesis. Pneumolysin can also activate the classical pathway of complement, and this appears to involve antibody binding (via Fc) by a region of the toxin homologous to C-reactive protein, a human acute-phase protein also capable of classical pathway activation and implicated in host defence against pneumococcal infection.",
keywords = "Amino Acid Sequence, Animals, Bacterial Proteins, C-Reactive Protein, Cell Membrane, Complement Pathway, Classical, Cysteine, Humans, Immunoglobulin Fc Fragments, Mice, Molecular Sequence Data, Mutagenesis, Site-Directed, Streptococcus pneumoniae, Streptolysins, Structure-Activity Relationship, Sulfhydryl Compounds, Virulence",
author = "Boulnois, {G J} and Paton, {J C} and Mitchell, {T J} and Andrew, {P W}",
year = "1991",
month = nov,
language = "English",
volume = "5",
pages = "2611--6",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley",
number = "11",

}

RIS

TY - JOUR

T1 - Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae

AU - Boulnois, G J

AU - Paton, J C

AU - Mitchell, T J

AU - Andrew, P W

PY - 1991/11

Y1 - 1991/11

N2 - Pneumolysin is a thiol-activated, membrane-damaging, multifunctional toxin and a known virulence factor of Streptococcus pneumoniae. The toxin can interfere with the functioning of both cellular and soluble components of the human immune system which protects against pneumococcal infection. Different amino acids within the toxin which are important in promoting oligomerization of the toxin in membranes and for the generation of functional lesions have been identified by site-directed mutagenesis. Pneumolysin can also activate the classical pathway of complement, and this appears to involve antibody binding (via Fc) by a region of the toxin homologous to C-reactive protein, a human acute-phase protein also capable of classical pathway activation and implicated in host defence against pneumococcal infection.

AB - Pneumolysin is a thiol-activated, membrane-damaging, multifunctional toxin and a known virulence factor of Streptococcus pneumoniae. The toxin can interfere with the functioning of both cellular and soluble components of the human immune system which protects against pneumococcal infection. Different amino acids within the toxin which are important in promoting oligomerization of the toxin in membranes and for the generation of functional lesions have been identified by site-directed mutagenesis. Pneumolysin can also activate the classical pathway of complement, and this appears to involve antibody binding (via Fc) by a region of the toxin homologous to C-reactive protein, a human acute-phase protein also capable of classical pathway activation and implicated in host defence against pneumococcal infection.

KW - Amino Acid Sequence

KW - Animals

KW - Bacterial Proteins

KW - C-Reactive Protein

KW - Cell Membrane

KW - Complement Pathway, Classical

KW - Cysteine

KW - Humans

KW - Immunoglobulin Fc Fragments

KW - Mice

KW - Molecular Sequence Data

KW - Mutagenesis, Site-Directed

KW - Streptococcus pneumoniae

KW - Streptolysins

KW - Structure-Activity Relationship

KW - Sulfhydryl Compounds

KW - Virulence

M3 - Article

C2 - 1779752

VL - 5

SP - 2611

EP - 2616

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 11

ER -