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Expression in Escherichia coli of the lpd A gene, protein sequence analysis and immunological characterization of the P64k protein from Neisseria meningitidis
Author(s) -
Guillén Gerardo,
Alvarez Anabel,
Silva Ricardo,
Morera Vivian,
González Sonia,
Musacchio Alexis,
Besada Vladimir,
Coizeau Edelgis,
Caballero Evelin,
Nazabal Consuelo,
Carmenate Tania,
González Luis J.,
Estrada Regla,
Támbara Yanet,
Padrón Gabriel,
Herrera Luis
Publication year - 1998
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1998.tb00494.x
Subject(s) - neisseria meningitidis , recombinant dna , escherichia coli , biology , microbiology and biotechnology , neisseriaceae , monoclonal antibody , bacterial outer membrane , neisseria , gene , meningococcal disease , western blot , peptide sequence , sequence analysis , virology , antibody , bacteria , genetics , antibiotics
By making use of recombinant DNA technology it is possible to characterize meningococcal outer membrane proteins (OMPs) capable of stimulating a host immune response. The lpd A gene, which codes for an OMP (P64k) from Neisseria meningitidis , was cloned in Escherichia coli. The recombinant protein was recognized by sera from patients convalescing from meningococcal disease. The monoclonal antibodies obtained against the recombinant protein recognized the natural protein on a Western blot, and monoclonal antibody 114 was assayed in ELISA with a panel of 85 N. meningitidis strains. The protein was recognized in 81 strains (95.3%); the strains that were not recognized were neither epidemic nor isolated from systemic disease. The complete amino acid sequence of P64k was obtained by automatic sequencing and MS.