Bacterial and Arachnid Sphingomyelinases D: Comparison of Biophysical and Pathological Activities.
Sphingomyelinases D have only been identified in arachnid venoms, Corynebacteria, Arcanobacterium, Photobacterium and in the fungi Aspergillus and Coccidioides. The arachnid and bacterial enzymes share very low sequence identity and do not contain the HKD sequence motif characteristic of the phospholipase D superfamily, however, molecular modeling and circular dichroism of SMases D from Loxosceles intermedia and Corynebacterium pseudotuberculosis indicate similar folds. The phospholipase, hemolytic and necrotic activities and mice vessel permeabilities were compared and both enzymes possess the ability to hydrolyze phospholipids and also promote similar pathological reactions in the host suggesting the existence of a common underlying mechanism in tissue disruption. J. Cell. Biochem. 118:2053-2063, 2017. © 2016 Wiley Periodicals, Inc.
Department of Physics, Multiuser Center for Biomolecular Innovation, UNESP, São José do Rio Preto, SP, Brazil.
Ricardo Barros
RB
Mariutti
Department of Cell Biology, UFPR, Curitiba, PR, Brazil.
Daniele
D
Chaves-Moreira
Department of Cell Biology, UFPR, Curitiba, PR, Brazil.
Larissa
L
Vuitika
Department of Physics, Multiuser Center for Biomolecular Innovation, UNESP, São José do Rio Preto, SP, Brazil.
Ícaro Putinhon
ÍP
Caruso
Department of Physics, Multiuser Center for Biomolecular Innovation, UNESP, São José do Rio Preto, SP, Brazil.
Monika A
MA
Coronado
Institute of Biological Sciences, UFMG, Belo Horizonte, MG, Brazil.
Vasco A
VA
Azevedo
Brazilian Biosciences National Laboratory, LNBio, Campinas, SP, Brazil.
Mario T
MT
Murakami
Department of Cell Biology, UFPR, Curitiba, PR, Brazil.
Silvio Sanches
SS
Veiga
Department of Physics, Multiuser Center for Biomolecular Innovation, UNESP, São José do Rio Preto, SP, Brazil.
Raghuvir K
RK
Arni
D000595:Amino Acid Sequence; D000818:Animals; D060829:Arthropod Proteins / Q000235:genetics / Q000378:metabolism / Q000633:toxicity*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism / Q000633:toxicity*; D002199:Capillary Permeability / Q000187:drug effects*; D003001:Cloning, Molecular; D016925:Corynebacterium pseudotuberculosis / Q000737:chemistry* / Q000201:enzymology / Q000472:pathogenicity; D004912:Erythrocytes / Q000187:drug effects; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D006461:Hemolysis / Q000187:drug effects; D006736:Horses; D006801:Humans; D051379:Mice; D010727:Phosphoric Diester Hydrolases / Q000235:genetics / Q000378:metabolism / Q000633:toxicity*; D011817:Rabbits; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism / Q000633:toxicity; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D034561:Sheep, Domestic; D012867:Skin / Q000187:drug effects / Q000473:pathology; D013112:Spiders / Q000737:chemistry* / Q000201:enzymology / Q000472:pathogenicity
D060829:Arthropod Proteins; D001426:Bacterial Proteins; D011994:Recombinant Proteins; D010727:Phosphoric Diester Hydrolases; C055160:sphingomyelin phosphodiesterase D
CATALYSIS; DERMONECROSIS; HEMOLYSIS; SPHINGOMYELINASE D