Characterization of the receptor-binding domain of tetanus toxin
JL Halpern, A Loftus - Journal of Biological Chemistry, 1993 - ASBMB
The carboxyl-terminal half of the heavy chain of tetanus toxin (Hc) contains the domain
required for binding to purified gangliosides and neuronal cells. The structural requirements
for the interaction of Hc with receptor were studied by generating mutants of Hc with
deletions at either the carboxyl or amino terminus and characterizing their binding. A
deletion of 10 or more amino acids from the carboxyl terminus resulted in a major loss of Hc
binding to purified gangliosides and spinal cord neuronal cells, whereas a deletion of the …
required for binding to purified gangliosides and neuronal cells. The structural requirements
for the interaction of Hc with receptor were studied by generating mutants of Hc with
deletions at either the carboxyl or amino terminus and characterizing their binding. A
deletion of 10 or more amino acids from the carboxyl terminus resulted in a major loss of Hc
binding to purified gangliosides and spinal cord neuronal cells, whereas a deletion of the …