Dr. Jacob A Siedlik

The coronavirus disease of 2019 (COVID-19) pandemic is caused by the novel SARS-CoV-2 virus. Antibody responses develop against SARS-CoV-2 during the infection in many subjects tend to increase over the course of disease and correlate with viral RNA titer. HEK-293T cells were cultured in Dulbecco’s modified Eagle medium with 10% fetal bovine serum (FBS) and 1% penicillin–streptomycin. Cells expressing either the SARS-CoV-2 spike or nucleocapsid proteins were generated for use in the immunofluorescence assay and as target cells in the ADCC assay. The major implication of our findings is that efficacy of COVID-19 vaccine candidates should not be evaluated solely based on the level of nAb elicited, but rather the totality of SARS-CoV-2 specific humoral responses elicited.

Heat shock proteins (HSP) are chaperone molecules that are known to facilitate protein synthesis, protein assembly, provide cellular protection and regulate intracellular signaling. These cytoprotective effects have been linked to increases in HSP70 and HSP27p concentrations but there has been little progress in determining the specific role of HSP in human skeletal muscle adaptations. Short wave diathermy (SWD) and ultrasound are treatments commonly used to stimulate deep heat increases in skeletal muscle with limited research examining the effects of increased muscle temperature on muscle damage induced injury severity. Current research cannot definitively identify the mechanistic roles of HSP in mitigation of muscle damage even though they are commonly cited as mechanism of action for prevention of damage in heat-treated muscle. This article will examine the role of HSP induction in skeletal muscle as a therapeutic countermeasure for reduction of muscle atrophy during prolonged periods of immobilization as well as mechanisms for accelerated repair of injured muscle fibers through increased total protein concentrations.