A monoclonal antibody recognizing the p150/95 leucocyte differentiation antigen

Area of Science:

• Immunology
• Cell Biology
• Biochemistry

Background:

• Leukocyte differentiation antigens play crucial roles in immune cell function and identification.
• The p150/95 molecule is part of a family of adhesion molecules involved in immune responses.
• Understanding the specific epitopes recognized by antibodies is vital for precise cell characterization.

Purpose of the Study:

• To describe a novel monoclonal antibody, KB90, and its target molecule.
• To characterize the binding epitope of KB90 on the target molecule.
• To determine the immunocytochemical reactivity profile of KB90 on various immune cells and compare it to related molecules.

Main Methods:

• Biochemical dissociation of the target molecule under high pH conditions.
• Epitope mapping using the monoclonal antibody KB90.
• Immunocytochemical analysis of KB90 reactivity on human leukocytes and tissue macrophages.

Main Results:

• Monoclonal antibody KB90 recognizes a molecule composed of 140 kd and 98 kd polypeptide subunits.
• KB90 binds to an epitope on the 140 kd subunit after dissociation.
• The recognized molecule is identified as p150/95, a member of the leukocyte differentiation antigen family.
• Immunocytochemical staining revealed KB90 reactivity on monocytes, macrophages, granulocytes, and a subset of lymphocytes.
• KB90 reactivity patterns are distinct from those observed for LFA-1 and Mac-1 molecules.

Conclusions:

• Monoclonal antibody KB90 is a valuable tool for identifying and characterizing the p150/95 leukocyte differentiation antigen.
• KB90 recognizes a specific epitope on the 140 kd subunit, differentiating it from LFA-1 and Mac-1.
• The distinct reactivity profile of KB90 provides new insights into the heterogeneity of immune cell populations.