Pathogenic homozygous mutations in SARS2 are associated with symptoms including premature birth and infant onset kidney failure, called HUPRA syndrome (Hyperuricemia, pulmonary hypertension, renal failure, and alkalosis syndrome).[9]
As with many mutations that affect protein translation,[10] mutations in SARS2 have been shown to cause a collection of diseases, such as hyperuricemia, metabolic alkalosis, pulmonary hypertension, and progressive kidney failure in infancy; together, these conditions are known as HUPRA syndrome.[11]
Some cases of missense mutations in SARS2 have been observed to result in a complete lack of acetylated seryl-tRNA synthetase and a severely reduced amount of non-acetylated enzyme.[11] This results in the ineffective or complete inability of L-serine to be transferred to its cognate tRNA, resulting in incomplete protein translation and folding. The impacts appear to only reach a phenotypic pathology in certain high energy expenditure cells, such as renal cells and lung tissue. It has been suggested that the residual activity of the SARS2 gene allows most other tissues to avoid cytopathic symptoms, however, is unable to protect high-energy requirement cells from damage.[11]
SARS2 mutations resulting in HUPRA syndrome are extremely rare, with less than 1 in 1,000,000 babies born with the condition.[12] A Palestinian community in the Greater Jerusalem region appears to have a much higher incidence of the mutation, potentially due to a common ancestor.[11]
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Gibbons WJ, Yan Q, Li R, et al. (2004). "Genomic organization, expression, and subcellular localization of mouse mitochondrial seryl-tRNA synthetase". Biochem. Biophys. Res. Commun. 317 (3): 774–8. Bibcode:2004BBRC..317..774G. doi:10.1016/j.bbrc.2004.03.113. PMID15081407.
