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The present study aimed to select an antigen of Lucilia sericata larvae showing both high antigenicity and cross-reactive binding abilities with other related antigens of L. sericata larvae for obtaining a promising candidate vaccine antigen. The ELISA results primary concluded that among the excretory secretory (ES) and midgut (MG) antigens of the different larval instars of L. sericata, MGL2 could be characterized as antigen which was able to reflect the highest level of antigenicity and cross-reactivity with the other tested L. sericata antigens. The results were extended to spot the light on the relation between different protein bands in MGL2 and rabbit hyper- immune sera (HIS) raised against the other tested antigens using SDS-PAGE and Western blot technique. Analysis by SDS-PAGE of ES and MG antigens of the different larval instars of L. sericata revealed common protein bands at molecular weights of about 10, 12, 16, 20, 28, 33 and 46 kDa. Western blotting of MGL2 antigen transferred to nitrocellulose sheet revealed reaction by MGL2 HIS to five polypeptide bands; 20, 28, 33, 46 and 63 kDa. Three bands of 28, 33 and 63 kDa were the most prominent bands detected whereas; there was a weak reaction with bands of 20 and 46 kDa. But what was apparent in Western blot was a strong reaction of all tested HIS with a polypeptide band of 63 kDa. This band might be considered to be the main cause of cross reactive binding ability of MGL2 antigen that had been recorded previously in ELISA technique. [ABSTRACT FROM AUTHOR]

Myelin basic protein (MBP) or a fragment thereof may enter cerebrospinal fluid (CSF) and other body fluids in an etiologically nonspecific fashion to provide information about the status of central nervous system (CNS) myelin damage. MBP immunochemically detected is referred to as MBP-like material (MBPLM). The clinical utility of the assay for MBPLM in CSF is to document the presence, continuation, or resolution of CNS myelin injury. The analysis of CSF for MBPLM is subject to many variables, among which are the antisera and the form of the assay utilized. The dominant epitope of CSF MBPLM is in the decapeptide of 80 – 89 from the intact MBP molecule of 170 residues. Normally, CSF has no detected MBPLM. Following an acute relapse of MS, MBPLM rises quickly in the range of ng/ml and rapidly declines and disappears. The presence of MBPLM in CSF in chronic and progressive phases of the disease is unusual, but it may sometimes be detected in low levels, depending on the assay used for detection. The level of CSF MBPLM is related to both the mass of CNS myelin damage and how recently it occurred. The level of CSF MBPLM rarely is elevated in optic neuritis. The level of CSF MBPLM is unrelated to CSF protein level, level of IgG, presence of oligoclonal bands or pleocytosis. CSF MBPLM has the potential of serving as a marker of therapeutic effectiveness in MS and does have predictive value for response to glucocorticoids given for worsening of disease. The detection of MBPLM in body fluids other than CSF would be of great value because of the resulting improved feasibility for objectively monitoring the natural history of MS and response to therapy. Studies on blood have yet to produce a valid assay of MBPLM. Urinary MBPLM, though different in its features from that in CSF, may provide a correlate, not with acute demyelination in MS as is the case for CSF, but with progression of disease. [ABSTRACT FROM AUTHOR]

Reviews the techniques of peripheral blood progenitor cell (PBPC) collection, mobilization, purification and ex vivo expansion. Leukaphereris machines employed for PBPC; Chemotherapy-induced mobilization of PBPC; Tumor cell contamination of PBPC grafts.