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Polyreactive Binding of Antibodies Generated by Polyclonal B Cell Activation. II. Crossreactive and Monospecific Antibodies can be Generated from an Identical Ig Rearrangement by Differential Glycosylation by C. FERNÁNDEZ; M. E. ALARCÓN‐RIQUELME; E. SVERREMARK is a Immunology and Microbiology article available to read on EtoBox.

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In this work the authors tested the hypothesis that differential glycosylation may be one of the mechanisms by which B cells could be able to produce monospecific or polyreactive antibodies flexibly. The same genetic information will be used in both situations. To prove this hypothesis the authors used mice transgenic for the SP6 (μ+κ) hybridoma cell line producing monoclonal antibodies (MoAbs) with specificity for the hapten 2,4,6‐trinitrophenyl (TNP). In these animals most cells in the periphery express exclusively the transgene SP6. To obtain polyreactive antibodies (Abs) spleen cells from transgenic animals were stimulated __in vitro__ with lipopolysaccharide (LPS). The authors used LPS derived B cell blasts to produce a hybridoma cell collection. A high proportion of the monoclonal antibodies were found to bind to TNP and to crossreact with unrelated antigens. Endogenous immunoglobulins (lgs) were not responsible for crossreactivity since the crossreactive clones only expressed the transgene products. This was demonstrated by polymerase chain reaction (PCR) amplification of cDNA and by sequencing analysis of the PCR products. The nucleotide sequences of the expressed mono‐ and

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Author

C. FERNÁNDEZ; M. E. ALARCÓN‐RIQUELME; E. SVERREMARK

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0300-9475)

Published

1997

Language

EN

Field

Immunology and Microbiology (Life Sciences)