Recombinant PhpA Protein, a Unique Histidine Motif-Containing Protein from Streptococcus pneumoniae, Protects Mice against Intranasal Pneumococcal Challenge
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Published in | Infection and Immunity Vol. 69; no. 6; pp. 3827 - 3836 |
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AbstractList | The multivalent pneumococcal conjugate vaccine is effective against both systemic disease and otitis media caused by serotypes contained in the vaccine. However, serotypes not covered by the current conjugate vaccine may still cause pneumococcal disease. To address these serotypes and the remaining otitis media due to Streptococcus pneumoniae, we have been evaluating antigenically conserved proteins from S. pneumoniae as vaccine candidates. A previous report identified a 20-kDa protein with putative human complement C3-proteolytic activity. By utilizing the publicly released pneumococcal genomic sequences, we found the gene encoding the 20-kDa protein to be part of a putative open reading frame of approximately 2,400 bp. We recombinantly expressed a 79-kDa fragment (rPhpA-79) that contains a repeated HxxHxH motif and evaluated it for vaccine potential. The antibodies elicited by the purified rPhpA-79 protein were cross-reactive to proteins from multiple strains of S. pneumoniae and were against surface-exposed epitopes. Immunization with rPhpA-79 protein adjuvanted with monophosphoryl lipid A (for subcutaneous immunization) or a mutant cholera toxin, CT-E29H (for intranasal immunization), protected CBA/N mice against death and bacteremia, as well as reduced nasopharyngeal colonization, following intranasal challenge with a heterologous pneumococcal strain. In contrast, immunization with the 20-kDa portion of the PhpA protein did not protect mice. These results suggest that rPhpA-79 is a potential candidate for use as a vaccine against pneumococcal systemic disease and otitis media. ABSTRACT The multivalent pneumococcal conjugate vaccine is effective against both systemic disease and otitis media caused by serotypes contained in the vaccine. However, serotypes not covered by the current conjugate vaccine may still cause pneumococcal disease. To address these serotypes and the remaining otitis media due to Streptococcus pneumoniae , we have been evaluating antigenically conserved proteins from S. pneumoniae as vaccine candidates. A previous report identified a 20-kDa protein with putative human complement C3-proteolytic activity. By utilizing the publicly released pneumococcal genomic sequences, we found the gene encoding the 20-kDa protein to be part of a putative open reading frame of approximately 2,400 bp. We recombinantly expressed a 79-kDa fragment (rPhpA-79) that contains a repeated HxxHxH motif and evaluated it for vaccine potential. The antibodies elicited by the purified rPhpA-79 protein were cross-reactive to proteins from multiple strains of S. pneumoniae and were against surface-exposed epitopes. Immunization with rPhpA-79 protein adjuvanted with monophosphoryl lipid A (for subcutaneous immunization) or a mutant cholera toxin, CT-E29H (for intranasal immunization), protected CBA/N mice against death and bacteremia, as well as reduced nasopharyngeal colonization, following intranasal challenge with a heterologous pneumococcal strain. In contrast, immunization with the 20-kDa portion of the PhpA protein did not protect mice. These results suggest that rPhpA-79 is a potential candidate for use as a vaccine against pneumococcal systemic disease and otitis media. Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue IAI About IAI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy Connect to IAI IAI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0019-9567 Online ISSN: 1098-5522 Copyright © 2014 by the American Society for Microbiology. For an alternate route to IAI .asm.org, visit: IAI The multivalent pneumococcal conjugate vaccine is effective against both systemic disease and otitis media caused by serotypes contained in the vaccine. However, serotypes not covered by the current conjugate vaccine may still cause pneumococcal disease. To address these serotypes and the remaining otitis media due to Streptococcus pneumoniae , we have been evaluating antigenically conserved proteins from S. pneumoniae as vaccine candidates. A previous report identified a 20-kDa protein with putative human complement C3-proteolytic activity. By utilizing the publicly released pneumococcal genomic sequences, we found the gene encoding the 20-kDa protein to be part of a putative open reading frame of approximately 2,400 bp. We recombinantly expressed a 79-kDa fragment (rPhpA-79) that contains a repeated HxxHxH motif and evaluated it for vaccine potential. The antibodies elicited by the purified rPhpA-79 protein were cross-reactive to proteins from multiple strains of S. pneumoniae and were against surface-exposed epitopes. Immunization with rPhpA-79 protein adjuvanted with monophosphoryl lipid A (for subcutaneous immunization) or a mutant cholera toxin, CT-E29H (for intranasal immunization), protected CBA/N mice against death and bacteremia, as well as reduced nasopharyngeal colonization, following intranasal challenge with a heterologous pneumococcal strain. In contrast, immunization with the 20-kDa portion of the PhpA protein did not protect mice. These results suggest that rPhpA-79 is a potential candidate for use as a vaccine against pneumococcal systemic disease and otitis media. |
Author | Ying Zhang Vicki Barniak Amy W. Masi Ken Mountzouros Margaret K. Hostetter Bruce A. Green |
AuthorAffiliation | Departments of Immunology 1 and Bacteriology 2 Research, Wyeth Lederle Vaccines, West Henrietta, New York, and Department of Children's Health, Yale University School of Medicine, New Haven, Connecticut 3 |
AuthorAffiliation_xml | – name: Departments of Immunology 1 and Bacteriology 2 Research, Wyeth Lederle Vaccines, West Henrietta, New York, and Department of Children's Health, Yale University School of Medicine, New Haven, Connecticut 3 |
Author_xml | – sequence: 1 surname: YING ZHANG fullname: YING ZHANG organization: Department of Immunology, Wyeth Lederle Vaccines, West Henrietta, New York, United States – sequence: 2 givenname: Amy W surname: MASI fullname: MASI, Amy W organization: Department of Bacteriology Research, Wyeth Lederle Vaccines, West Henrietta, New York, United States – sequence: 3 givenname: Vicki surname: BARNIAK fullname: BARNIAK, Vicki organization: Department of Immunology, Wyeth Lederle Vaccines, West Henrietta, New York, United States – sequence: 4 givenname: Ken surname: MOUNTZOUROS fullname: MOUNTZOUROS, Ken organization: Department of Bacteriology Research, Wyeth Lederle Vaccines, West Henrietta, New York, United States – sequence: 5 givenname: Margaret K surname: HOSTETTER fullname: HOSTETTER, Margaret K organization: Department of Children's Health, Yale University School of Medicine, New Haven, Connecticut, United States – sequence: 6 givenname: Bruce A surname: GREEN fullname: GREEN, Bruce A organization: Department of Bacteriology Research, Wyeth Lederle Vaccines, West Henrietta, New York, United States |
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Cites_doi | 10.1016/S0021-9258(19)52451-6 10.4049/jimmunol.161.8.4115 10.1097/00006454-200004000-00036 10.1016/S0898-6568(97)00175-7 10.1016/S0264-410X(99)00530-7 10.1016/S0140-6736(05)62222-2 10.1086/315388 10.1128/iai.62.1.319-324.1994 10.1093/nar/7.6.1513 10.1089/mdr.1999.5.85 10.1016/S0264-410X(00)00058-X 10.1128/IAI.68.2.796-800.2000 10.1016/S0002-9343(99)00105-9 10.1128/iai.58.10.3293-3299.1990 10.1111/j.1365-2958.1997.mmi494.x 10.1086/315722 10.1086/513980 10.1093/infdis/170.3.600 10.1006/mpat.1996.0038 10.1038/227680a0 10.1128/jb.156.1.281-290.1983 10.1093/infdis/153.4.682 10.1084/jem.160.2.386 10.1086/313608 10.1093/infdis/148.1.131 10.1046/j.1365-2958.1997.5111879.x 10.1074/jbc.273.36.22957 10.1111/j.1530-0277.1997.tb04500.x |
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Keywords | Still disease Middle ear disease Diseases of the osteoarticular system Systemic Histidine Antigenicity Streptococcal infection Systemic disease Bacteria Micrococcales ENT disease Recombinant protein Serotype Anthropogenic factor Human Rodentia Vaccine Protein A Streptococcus pneumoniae Infection Streptococcaceae Vertebrata Mammalia Mouse Aminoacid Bacteriosis Otitis media Conjugation |
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Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Corresponding author. Mailing address: Wyeth-Lederle Vaccines, 211 Bailey Rd., West Henrietta, NY 14586-9728. Phone: (716) 273-7681. Fax: (716) 273-7515. E-mail: zhangy4@war.wyeth.com. |
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SubjectTerms | Administration, Intranasal Animals Antibodies, Bacterial - blood Bacterial diseases Bacterial Proteins - genetics Bacterial Proteins - immunology Bacteriology Biological and medical sciences Endopeptidases - chemistry Endopeptidases - genetics Endopeptidases - immunology Endopeptidases - metabolism Experimental bacterial diseases and models Fundamental and applied biological sciences. Psychology Histidine - chemistry Humans Immunization Infectious diseases Male Medical sciences Mice Mice, Inbred CBA Microbial Immunity and Vaccines Microbiology Molecular Sequence Data Nasopharynx - microbiology Otitis Media - microbiology Otitis Media - prevention & control PhpA protein Pneumococcal Infections - microbiology Pneumococcal Infections - prevention & control Pneumococcal Vaccines - immunology Recombinant Proteins - genetics Recombinant Proteins - immunology Recombinant Proteins - metabolism Sequence Analysis, DNA Streptococcal Vaccines Streptococcus pneumoniae Streptococcus pneumoniae - immunology Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies |
Title | Recombinant PhpA Protein, a Unique Histidine Motif-Containing Protein from Streptococcus pneumoniae, Protects Mice against Intranasal Pneumococcal Challenge |
URI | http://iai.asm.org/content/69/6/3827.abstract https://www.ncbi.nlm.nih.gov/pubmed/11349048 https://search.proquest.com/docview/17867967 https://search.proquest.com/docview/70849700 https://pubmed.ncbi.nlm.nih.gov/PMC98401 |
Volume | 69 |
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