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The emergence of the RNA virus SARS-CoV2, the causative agent of COVID-19 and its declaration by the World Health Organization (WHO) as a pandemic has disrupted the delicate balance in health indices globally. Its attendant immune dysregulation and pathobiology is still evolving. Currently, real time PCR is the gold standard diagnostic test, however there are several invalidated antibody-based tests available for possible community screening. With ongoing community transmission in Nigeria, neither the true burden of COVID-19 nor the performance of these kits is presently known. This study therefore, compared the performance of the SARS CoV2 antibody test and the real time Polymerase Chain Reaction (Rt-PCR) in the diagnosis of COVID-19. For the purpose of this evaluation, we used the diagnostic test kit by Innovita® Biological Technology CO., LTD China, a total of 521 venous blood samples were collected from consenting patients for the SARS COVID-19 rapid diagnostic kit and Oral and Nasopharyngeal swabs were collected and analyzed using the real time Polymerase chain reaction technique for nucleic acid detection and quantification.

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The alteration of whole Sendai virus and especially of its nucleocapsid polypeptides, during storage of the virus at 4 degree C in the allantoic fluids in which it was cultivated, has cultivated, has been studied by sodium dodecyl sulfate gel electrophoresis. During virus storage the nucleocapsid protein subunits with a molecular weight of 60,000 and the putative inner envelope protein with a molecular weight of 38,000 were mainly affected. Both virus components were partially degraded to smaller components. Examination of nucleocapsids isolated from "stored" virus showed that, in addition to the 60,000-molecular weight polypetide component, a smaller polypeptide component with a molecular weight of 46,000 appeared. The relative proportion of the small component increased with the storage period: a kind of specific conversion of large to small components occurred during storage. Since viruses kept in the absence of allantoic fluids revealed no similar modifications of their polypeptides, we concluded that a cellular component present in the allantoic fluids - very likely of enzymatic nature - is responsible for the observed cleavage of virus polypeptides.

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