Vaccine Potential of theNeisseria meningitidis2086 Lipoprotein
| Autor: | Robert P. Smith, Alan Howell, Peggy Ooi, Vicki Barniak, Paige Weise, John Farley, Xiaoling Xie, Leah Diane Fletcher, Liesel A. Bernfield, Robert J. Zagursky, Gary W. Zlotnick, Melissa Knauf, Ying Zhang, Mike Wetherell |
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| Rok vydání: | 2004 |
| Předmět: |
Lipoproteins
Molecular Sequence Data Immunology Meningococcal Vaccines Cross Reactions Neisseria meningitidis Serogroup B Biology medicine.disease_cause Microbiology Mice Bacterial Proteins Protein purification medicine Animals Humans Amino Acid Sequence Peptide sequence Antigens Bacterial Neisseria meningitidis Sequence Analysis DNA Flow Cytometry biology.organism_classification Antibodies Bacterial Recombinant Proteins Meningococcal Infections Infectious Diseases Microbial Immunity and Vaccines Neisseria lactamica Neisseria gonorrhoeae Female Immunization Parasitology Neisseriaceae Neisseria Bacterial outer membrane |
| Zdroj: | Infection and Immunity. 72:2088-2100 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.72.4.2088-2100.2004 |
| Popis: | A novel antigen that induces cross-reactive bactericidal antibodies against a number ofNeisseria meningitidisstrains is described. This antigen, a ∼28-kDa lipoprotein called LP2086, was first observed within a complex mixture of soluble outer membrane proteins (sOMPs) following a series of fractionation, protein purification, and proteomics steps. Approximately 95 different neisserial isolates tested positive by Western blotting and PCR screening methods for the presence of the protein and the gene encoding LP2086. The strains tested included isolates ofN. meningitidisserogroups A, B, C, W135, and Y,Neisseria gonorrhoeae, andNeisseria lactamica. To better understand the microheterogeneity of this protein, the 2086 genes from 63 neisserial isolates were sequenced. Two different subfamilies of LP2086 were identified based on deduced amino acid sequence homology. A high degree of amino acid sequence similarity exists within each 2086 subfamily. The highest degree of genetic diversity was seen between the two subfamilies which share approximately 60 to 75% homology at the nucleic acid level. Flow cytometry (fluorescence-activated cell sorting) analyses and electron microscopy indicated that the LP2086 is localized on the outer surface ofN. meningitidis. Antiserum produced against a single protein variant was capable of eliciting bactericidal activity against strains expressing different serosubtype antigens. Combining one recombinant lipidated 2086 (rLP2086) variant from each subfamily with two rPorA variants elicited bactericidal activity against all strains tested. The rLP2086 family of antigens are candidates worthy of further vaccine development. |
| Databáze: | OpenAIRE |
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