Comparative anatomy of the brachial plexus and shoulder nerves of theSapajus
JOURNAL OF MEDICAL PRIMATOLOGY
Authors: Figueredo-da-Silva, Sylla; Vasconcelos-da-Silva, Ediana; Abreu, Taina; Aversi-Ferreira, Tales Alexandre
Abstract
Background The capuchin is a neotropical primate that presents easy reproduction in captivity and is used in scientific research. The objective of this work was to describe the structure and the branching pattern of the brachial plexus of the capuchin and to compare the results with data from the literature for humans, chimpanzees, baboons andCallithrix. Methods Twelve specimens were used: eight males and four females. No animals were killed for the purpose of this study. Results The brachial plexus ofSapajussp was constituted mainly from the ventral roots of the last four cervical spinal nerves, from C5 to C8, mainly, and the first thoracic nerve (T1). Conclusions The pattern of formation of the brachial plexus of the capuchin monkey was more similar to that ofCallithrixand baboons, perhaps because they are the only primates in this study to be essentially quadrupedal.
Interference of the Zika Virus E-Protein With the Membrane Attack Complex of the Complement System
FRONTIERS IN IMMUNOLOGY
Authors: Malekshahi, Zahra; Schiela, Britta; Bernklau, Sarah; Banki, Zoltan; Wuerzner, Reinhard; Stoiber, Heribert
Abstract
The complement system has developed different strategies to clear infections by several effector mechanisms, such as opsonization, which supports phagocytosis, attracting immune cells by C3 and C5 cleavage products, or direct killing of pathogens by the formation of the membrane attack complex (MAC). As the Zika virus (ZIKV) activates the classical complement pathway and thus has to avoid clearance by the complement system, we analyzed putative viral escape mechanisms, which limit virolysis. We identified binding of the recombinant viral envelope E protein to components of the terminal pathway complement (C5b6, C7, C8, and C9) by ELISA. Western blot analyses revealed that ZIKV E protein interfered with the polymerization of C9, induced on cellular surfaces, either by purified terminal complement proteins or by normal human serum (NHS) as a source of the complement. Further, the hemolytic activity of NHS was significantly reduced in the presence of the recombinant E protein or entire viral particles. This data indicates that ZIKV reduces MAC formation and complement-mediated lysis by binding terminal complement proteins to the viral E protein.