Advanced

Human monoclonal antibodies against an epitope on the class 5c outer membrane protein common to many pathogenic strains of Neisseria meningitidis

De Cossío, Maria E Fernández; Ohlin, Mats LU ; Llano, Manual; Selander, Barbro LU ; Cruz, Silian; Del Valle, Jesus and Borrebaeck, Carl A K LU (1992) In Journal of Infectious Diseases 166(6). p.1322-1328
Abstract

Neisseria meningitidis is a causative agent of meningitis. Despite vaccination programs, it still causes a large number of deaths in young children. Early diagnosis followed by passive immunization with human monoclonal antibodies could be an approach to effective therapy. Peripheral blood lymphocytes from normal, healthy blood donors and from vaccinated individuals were immunized in vitro, using outer membrane proteins purified from A. meningitidis B:4:P1,15. The immunized human B cells were Epstein-Barr virus transformed and fused to a heteromyeloma. Several stable human hybridoma cell lines were established and two, secreting antibodies against the 31-kDa class 5c outer membrane protein, were characterized further. The human... (More)

Neisseria meningitidis is a causative agent of meningitis. Despite vaccination programs, it still causes a large number of deaths in young children. Early diagnosis followed by passive immunization with human monoclonal antibodies could be an approach to effective therapy. Peripheral blood lymphocytes from normal, healthy blood donors and from vaccinated individuals were immunized in vitro, using outer membrane proteins purified from A. meningitidis B:4:P1,15. The immunized human B cells were Epstein-Barr virus transformed and fused to a heteromyeloma. Several stable human hybridoma cell lines were established and two, secreting antibodies against the 31-kDa class 5c outer membrane protein, were characterized further. The human antibodies were of IgG1 and IgG3 isotypes, with κ light chains. The recognized epitope was commonly found among pathogenic strains of N. meningitidis; thus, these human monoclonal antibodies may be important in the evaluation of N. meningitidis infections.

(Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Infectious Diseases
volume
166
issue
6
pages
7 pages
publisher
Oxford University Press
external identifiers
  • Scopus:0026489196
ISSN
0022-1899
DOI
10.1093/infdis/166.6.1322
language
English
LU publication?
yes
id
052dfd88-b119-4c95-90e6-dae06dc82a4e
date added to LUP
2016-04-20 16:11:50
date last changed
2016-10-13 05:06:49
@misc{052dfd88-b119-4c95-90e6-dae06dc82a4e,
  abstract     = {<p>Neisseria meningitidis is a causative agent of meningitis. Despite vaccination programs, it still causes a large number of deaths in young children. Early diagnosis followed by passive immunization with human monoclonal antibodies could be an approach to effective therapy. Peripheral blood lymphocytes from normal, healthy blood donors and from vaccinated individuals were immunized in vitro, using outer membrane proteins purified from A. meningitidis B:4:P1,15. The immunized human B cells were Epstein-Barr virus transformed and fused to a heteromyeloma. Several stable human hybridoma cell lines were established and two, secreting antibodies against the 31-kDa class 5c outer membrane protein, were characterized further. The human antibodies were of IgG1 and IgG3 isotypes, with κ light chains. The recognized epitope was commonly found among pathogenic strains of N. meningitidis; thus, these human monoclonal antibodies may be important in the evaluation of N. meningitidis infections.</p>},
  author       = {De Cossío, Maria E Fernández and Ohlin, Mats and Llano, Manual and Selander, Barbro and Cruz, Silian and Del Valle, Jesus and Borrebaeck, Carl A K},
  issn         = {0022-1899},
  language     = {eng},
  number       = {6},
  pages        = {1322--1328},
  publisher    = {ARRAY(0xafaff78)},
  series       = {Journal of Infectious Diseases},
  title        = {Human monoclonal antibodies against an epitope on the class 5c outer membrane protein common to many pathogenic strains of Neisseria meningitidis},
  url          = {http://dx.doi.org/10.1093/infdis/166.6.1322},
  volume       = {166},
  year         = {1992},
}