Background Extensive studies have demonstrated that the inside-out membrane phospholipid phosphatidylserine (PS) actively drives global immunosuppression in the tumor microenvironment and is a major contributor to tumor resistance to immune checkpoint blockade. We have shown that PS targeting antibodies can re-program the tumor microenvironment from immunosuppressive to immune potentiating by r...

Most inhibitory antibodies to human factor VIII (fVIII) bind to epitopes in the A2, ap-A3, or C2 domains. The anticoagulant action of antibodies to the C2 domain is due to inhibition of binding of fVIII to phospholipid. The x-ray structure of the human fVIII C2 domain shows a putative hydrophobic, 3-prong, phospholipid membrane-binding site consisting of Met2199/ Phe2200, Val2223, and Leu2251/L...

Most inhibitory antibodies to human factor VIII (fVIII) bind to epitopes in the A2, ap-A3, or C2 domains. The anticoagulant action of antibodies to the C2 domain is due to inhibition of binding of fVIII to phospholipid. The x-ray structure of the human fVIII C2 domain shows a putative hydrophobic, 3-prong, phospholipid membrane-binding site consisting of Met2199/Phe2200, Val2223, and Leu2251/Le...

BACKGROUND The metabolic syndrome (MetS) is a proatherogenic entity. Autoantibodies to phospholipid cofactors such as beta2-glycoprotein I (beta2-gpI) can influence atheroma appearance. Previous studies confirmed an association of IgA anti-beta2-gpI antibodies with cerebral ischemia, myocardial infarction, peripheral artery disease and carotid disease. OBJECTIVE This case-control study evalua...

Prothrombin contains two kringle domains that are removed during activation to the blood clotting enzyme alpha-thrombin. By analogy with other kringle-containing proteins the prothrombin kringles may play a role in the protein-protein interactions necessary for prothrombin activation. Four monoclonal antibodies to prothrombin kringle 2 have been produced against human prothrombin, and a fifth m...

A patient with the anti-phospholipid antibody syndrome and digital clubbing is described. No recognized cause for the clubbing was found. It is suggested that platelet aggregation and microthrombi formation as a result of anti-phospholipid antibody may be involved in the pathogenesis of the digital clubbing. This may be a new feature of the anti-phospholipid antibody.

The diversity of factor VIII (fVIII) C2 domain antibody epitopes was investigated by competition enzyme-linked immunosorbent assay (ELISA) using a panel of 56 antibodies. The overlap patterns produced 5 groups of monoclonal antibodies (MAbs), designated A, AB, B, BC, and C, and yielded a set of 18 distinct epitopes. Group-specific loss of antigenicity was associated with mutations at the Met219...