| dc.description.abstract | Loxoscelism is a recognized public health problem in Brazil, but the venom
from Loxosceles similis (Moenkhaus, 1898) spider, which is widespread in Brazil due
to its adaptability to the urban environment, remains poorly characterized. Loxtox is a
family of phospholipase D enzymes (PLDs), which are the major components of
Loxosceles venom and are responsible for the clinical effects of loxoscelism. Loxtox
toxins correspond to 15% of L. similis (Moenkhaus, 1898) venom gland transcripts,
but the Loxtox family of L. similis (Moenkhaus, 1898) has yet to be fully described. In
this study, we aimed the functional charactereization of recombinant Loxtox and to
analyze their immunological properties in order to obtain antibodies able to neutralize
the effects evocked by L. similis (Moenkhaus, 1898) venom. Thus, we cloned and
functionally characterized recLoxtox s1A and recLoxtox s11A. These recombinant
toxins exhibited different in vitro activities depending on pH, and recLoxtox s1A had
more intense effects on rabbit skin than did recLoxtox s11A in vivo. Both recombinant
toxins were used in immunization protocols, and mapping of their epitopes revealed
different immunological reactions for the produced immune serums. Additionally,
polyclonal antibodies raised against recLoxtox s1A had greater capacity to
significantly reduce the in vitro and in vivo effects of L. similis (Moenkhaus, 1898)
venom. In summary, we obtained and characterized two novel Loxtox isoforms from
L. similis (Moenkhaus, 1898) venom, which may be valuable biotechnological and
immunological tools against loxoscelism. | |
