Intranasal immunization with recombinant group a streptococcal m protein fragment fused to the b subunit of escherichia coli labile toxin protects mice against systemic challenge infections

James Dale, Elbert C. Chiang

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

A fusion gene named LT-B-M5 was constructed encoding the entire B subunit of Escherichia coli labile toxin (LT-B), a 7 amino acid proline-rich linker, and 15 amino-terminal amino acids of type 5 streptococcal M protein. The purified LT-B-M5 was immunogenic in rabbits and evoked antibodies against a synthetic peptide copy of the amino-terminus of M5 (SM5[1-15]) and the native M5 protein and opsonic antibodies against type 5 streptococci. The hybrid protein retained the ganglioside-binding activity of LT-B and was tested in mice for its immunogenicity after local administration. Mice that were immunized intranasally with LT-B-M5 developed serum antibodies against SM5(1-15) and were significantly protected from death after intraperitoneal challenge infections with type 5 streptococci. The data show that protective systemic immune responses may be evoked after intranasal immunization with a fragment of M protein fused to LT-B.

Original languageEnglish (US)
Pages (from-to)1038-1041
Number of pages4
JournalJournal of Infectious Diseases
Volume171
Issue number4
DOIs
StatePublished - Jan 1 1995

Fingerprint

Immunization
Escherichia coli
Streptococcus
Antibodies
Infection
Amino Acids
Proteins
Gangliosides
Gene Fusion
Proline
Rabbits
Peptides
Serum
streptococcal M protein

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Infectious Diseases

Cite this

@article{b9e1420ebd9f47f6bae88418ece2a2b8,
title = "Intranasal immunization with recombinant group a streptococcal m protein fragment fused to the b subunit of escherichia coli labile toxin protects mice against systemic challenge infections",
abstract = "A fusion gene named LT-B-M5 was constructed encoding the entire B subunit of Escherichia coli labile toxin (LT-B), a 7 amino acid proline-rich linker, and 15 amino-terminal amino acids of type 5 streptococcal M protein. The purified LT-B-M5 was immunogenic in rabbits and evoked antibodies against a synthetic peptide copy of the amino-terminus of M5 (SM5[1-15]) and the native M5 protein and opsonic antibodies against type 5 streptococci. The hybrid protein retained the ganglioside-binding activity of LT-B and was tested in mice for its immunogenicity after local administration. Mice that were immunized intranasally with LT-B-M5 developed serum antibodies against SM5(1-15) and were significantly protected from death after intraperitoneal challenge infections with type 5 streptococci. The data show that protective systemic immune responses may be evoked after intranasal immunization with a fragment of M protein fused to LT-B.",
author = "James Dale and Chiang, {Elbert C.}",
year = "1995",
month = "1",
day = "1",
doi = "10.1093/infdis/171.4.1038",
language = "English (US)",
volume = "171",
pages = "1038--1041",
journal = "Journal of Infectious Diseases",
issn = "0022-1899",
publisher = "Oxford University Press",
number = "4",

}

TY - JOUR

T1 - Intranasal immunization with recombinant group a streptococcal m protein fragment fused to the b subunit of escherichia coli labile toxin protects mice against systemic challenge infections

AU - Dale, James

AU - Chiang, Elbert C.

PY - 1995/1/1

Y1 - 1995/1/1

N2 - A fusion gene named LT-B-M5 was constructed encoding the entire B subunit of Escherichia coli labile toxin (LT-B), a 7 amino acid proline-rich linker, and 15 amino-terminal amino acids of type 5 streptococcal M protein. The purified LT-B-M5 was immunogenic in rabbits and evoked antibodies against a synthetic peptide copy of the amino-terminus of M5 (SM5[1-15]) and the native M5 protein and opsonic antibodies against type 5 streptococci. The hybrid protein retained the ganglioside-binding activity of LT-B and was tested in mice for its immunogenicity after local administration. Mice that were immunized intranasally with LT-B-M5 developed serum antibodies against SM5(1-15) and were significantly protected from death after intraperitoneal challenge infections with type 5 streptococci. The data show that protective systemic immune responses may be evoked after intranasal immunization with a fragment of M protein fused to LT-B.

AB - A fusion gene named LT-B-M5 was constructed encoding the entire B subunit of Escherichia coli labile toxin (LT-B), a 7 amino acid proline-rich linker, and 15 amino-terminal amino acids of type 5 streptococcal M protein. The purified LT-B-M5 was immunogenic in rabbits and evoked antibodies against a synthetic peptide copy of the amino-terminus of M5 (SM5[1-15]) and the native M5 protein and opsonic antibodies against type 5 streptococci. The hybrid protein retained the ganglioside-binding activity of LT-B and was tested in mice for its immunogenicity after local administration. Mice that were immunized intranasally with LT-B-M5 developed serum antibodies against SM5(1-15) and were significantly protected from death after intraperitoneal challenge infections with type 5 streptococci. The data show that protective systemic immune responses may be evoked after intranasal immunization with a fragment of M protein fused to LT-B.

UR - http://www.scopus.com/inward/record.url?scp=0028958930&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028958930&partnerID=8YFLogxK

U2 - 10.1093/infdis/171.4.1038

DO - 10.1093/infdis/171.4.1038

M3 - Article

VL - 171

SP - 1038

EP - 1041

JO - Journal of Infectious Diseases

JF - Journal of Infectious Diseases

SN - 0022-1899

IS - 4

ER -