Biological activity of serum antibodies to a nonacylated form of lipoprotein D of Haemophilus influenzae
Författare
Summary, in English
Protein D, a surface-exposed 42-kDa membrane lipoprotein, is well conserved among both type b and nontypeable Haemophilus influenzae strains, and it is considered a vaccine against H. influenzae infections. Here, we report the large-scale purification of a nonacylated form of protein D (PDm) from the periplasmic space of Escherichia coli overexpressing PDm. Screening of human sera for levels of antibodies to PDm demonstrated that the immunoglobulin G (IgG) antibody level is above background levels in infants less than 6 months of age. Following a drop to background values in the age group 6 months to 1 year, IgG antibody levels start to increase, together with IgA antibody levels, after 1 year of age. The first appearance of serum IgM antibodies is in 6-month- to 1-year-old infants whose IgG antibody levels have dropped to the postnatal background level. Affinity-purified antibodies from humans and from PDm-immunized rats detected epitopes of protein D which are normally exposed on the bacterial surface. Affinity-isolated human anti-PDm antibodies eluted in acidic buffer were not bactericidal against H. influenzae. Loss of bactericidal activity may occur in this buffer, as was demonstrated in pooled human sera with high bactericidal activity after incubation in the same buffer. Hyperimmunization of rats with PDm induced high levels of serum IgG and IgA antibodies against PDm and significant bactericidal activity against homologous and heterologous H. influenzae strains.
Avdelning/ar
Publiceringsår
1996
Språk
Engelska
Sidor
4586-4592
Publikation/Tidskrift/Serie
Infection and Immunity
Volym
64
Issue
11
Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
American Society for Microbiology
Ämne
- Microbiology in the medical area
Status
Published
Forskningsgrupp
- Clinical Microbiology, Malmö
ISBN/ISSN/Övrigt
- ISSN: 1098-5522