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Medientyp:
E-Artikel
Titel:
HumanAntibodies Specific for the High-Molecular-Weight Adhesion Proteins ofNontypeable Haemophilus influenzae Mediate OpsonophagocyticActivity
Beteiligte:
Winter, Linda E.;
Barenkamp, Stephen J.
Erschienen:
American Society for Microbiology, 2003
Erschienen in:Infection and Immunity
Sprache:
Englisch
DOI:
10.1128/iai.71.12.6884-6891.2003
ISSN:
0019-9567;
1098-5522
Entstehung:
Anmerkungen:
Beschreibung:
<jats:title>ABSTRACT</jats:title>
<jats:p>
The
HMW1- and HMW2-like adhesion proteins of nontypeable
<jats:italic>Haemophilus
influenzae</jats:italic>
are expressed by 75% of these strains, and
antibodies directed against these proteins are protective in animal
models of infection. The purpose of the present study was to define the
functional activity of human antibodies specific for these proteins in
an in vitro complement-dependent opsonophagocytic assay. Human
promyelocytic cell line HL-60 served as the source of phagocytic cells,
and a commercial preparation of intravenous immunoglobulin (IVIG)
served as the source of human antibodies. High-molecular-weight (HMW)
proteins were purified from four prototype nontypeable
<jats:italic>H.
influenzae</jats:italic>
strains and used to prepare solid-phase affinity
columns. IVIG was adsorbed on each column to remove strain-specific
anti-HMW antibodies and to allow recovery of affinity-purified anti-HMW
antibody fractions. Unadsorbed IVIG killed each of the prototype
strains at titers of 1:80 to 1:320. HMW-adsorbed sera demonstrated
fourfold decreases in opsonophagocytic titer against the homologous
strains compared to unadsorbed IVIG. Affinity-purified anti-HMW
antibody preparations demonstrated opsonophagocytic titers of 1:20 to
1:80 against the respective homologous strains and opsonophagocytic
titers as high as 1:80 against heterologous strains. None of the
affinity-purified anti-HMW antibody preparations was opsonophagocytic
for a representative nontypeable
<jats:italic>H. influenzae</jats:italic>
strain that did
not express HMW1- or HMW2-like proteins. These data demonstrate that
human antibodies specific for the HMW1/HMW2-like adhesion proteins of
nontypeable
<jats:italic>H. influenzae</jats:italic>
are opsonophagocytic and that such
antibodies recognize epitopes shared by the HMW proteins of unrelated
nontypeable
<jats:italic>H. influenzae</jats:italic>
strains. These results argue for
continued investigation of the HMW1/HMW2-like proteins as potential
vaccine candidates for prevention of disease due to
nontypeable
<jats:italic>H.
influenzae</jats:italic>
.
</jats:p>