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Development and Characterization of Monoclonal Antibodies to Staphylococcus aureus Capsule Type 5
Author(s) -
Fan Hongxia,
Brown Martha,
Kowalski Rose,
Cook James,
Kary Marcia,
Hepler Robert,
Secore Susan,
Zorman Julie,
Pancari Gregory,
Vora Kalpit,
Cope Leslie,
Caulfield Michael,
McNeely Tessie
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.2_supplement.669
Subject(s) - monoclonal antibody , biology , microbiology and biotechnology , staphylococcus aureus , antibody , bacterial capsule , isotype , in vitro , antigen , bacteria , immunology , virulence , biochemistry , genetics , gene
Antibiotic‐resistant Staphylococcus aureus can produce a multitude of diseases as a result of infection of various tissues in the body. This organism is covered by a polysaccharide capsule and the majority of clinical isolates have been found to produce either type 5 (CP5) or type 8 (CP8) capsules. Previous studies by this laboratory have demonstrated that specific anti‐CP8 murine monoclonal antibodies (mAbs) have high levels of killing activity when compared to an isotype control mAb in an in vitro opsonophagocytic killing (OPK) assay. Pre‐binding of CP8‐specific mAbs to the bacterial surface enhanced clearance of this organism and survival in Balb/c mice after intra‐peritoneal challenge with aCP8 producing strain. To continue the investigation of anti‐capsular antibodies, two CP5‐specific mAbs were generated by immunized spleen cell fusion with a mouse myeloma cell line. These mAbs were shown to only bind CP5 producing strains and did not cross‐react with CP8 producing strains. These mAbs were evaluated in the in vitro OPK assay and showed high levels of activity with CP5 strains. These CP5 mAbs were also shown to protect mice challenged with mAb‐coated bacteria. When compared, CP5 murine mAbs were as effective as the CP8 mAbs in OPK activity and survival of infected mice. These CP5‐specific mAbs should be further investigated for use in clearance of this organism.