Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0036690 (sepsis)
 59,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nonketotic hyperglycinemia (OMIM #605899), also known as glycine encephalopathy, is an autosomal recessive disorder of glycine metabolism caused by a defect in the glycine cleavage system. A term neonate developed progressive lethargy, muscular hypotonia, and respiratory insufficiency on day 2 after birth, but no overt clinical seizures. Amplitude-integrated electroencephalography indicated a continuous burst-suppression pattern. The diagnosis of nonketotic hyperglycinemia was made biochemically and was confirmed by genetic studies, which revealed two missense mutations (one not previously described) within the glycine decarboxylase gene, GLDC. Nonketotic hyperglycinemia should be incorporated into the differential diagnosis of neonatal hypotonia, to avoid an erroneous diagnosis of sepsis or hypoxic ischemic injury. Amplitude-integrated electroencephalography may be helpful in the initial assessment of severely sick and hypotonic neonates without overt clinical seizures, and may direct further diagnostic evaluation.
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PMID:A novel missense mutation in a neonate with nonketotic hyperglycinemia. 2093 83

Seven mAbs with specific reaction patterns against each of the four genotypes and eight subtypes of viral hemorrhagic septicemia virus (VHSV) were produced, aiming to establish an immunoassay for typing VHSV isolates according to their genotype. Among the mAbs, VHS-1.24 reacted with all genotypes except genotype Ie, whilst mAb VHS-9.23 reacted with all genotypes except genotype III. mAb VHS-3.80 reacted with genotypes Ib, Ic, Id and II. mAb VHS-7.57 reacted with genotypes II and IVa, and mAb VHS-5.18 with genotype Ib only. Interestingly, mAb VHS-3.75 reacted with all of the genotype III isolates except a rainbow trout-pathogenic isolate from the west coast of Norway, and reacted in addition with the IVb isolate, CA-NB00-01, from the east coast of the USA. Finally, mAb VHS-1.88 reacted with all genotype IVb isolates from the Great Lakes, but not with CA-NB00-01. In conclusion, we can distinguish between all four genotypes and between five of eight subtypes of VHSV by testing isolates in immunoassay using a panel of nine mAbs. By Western blotting and transfection of cell cultures, it was shown that mAb VHS-1.24 recognized an epitope on the viral phosphoprotein (P), whilst all others recognized antigenic determinants on the nucleoprotein (N). From amino acid alignments of the various genotypes and subtypes of VHSV isolates, it was possible to determine the epitope specificity of mAb VHS-1.24 to be aa 32-34 in the P-protein; the specificities of mAbs VHS-3.80, VHS-7.57 and VHS-3.75 were found to be aa 43 and 45-48, aa 117 and 121, and aa 103, 118 and 121 of the N-protein, respectively.
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PMID:Typing of viral hemorrhagic septicemia virus by monoclonal antibodies. 2297 20

The phosphoprotein (P) of viral hemorrhagic septicemia virus (VHSV) plays an essential role in viral replication by interconnecting the L protein and the N protein-RNA complex. In this study, to investigate the role of the N-terminal region of the P protein in viral replication, we mutated the first or the first and second or the first, second, and third ATG codon into TGA stop codons. The respective mutants were named P1, P2, and P3. Recombinant VHSVs containing each mutated P gene (rVHSV-P1, -P2, and -P3) were successfully generated by supplying the intact P protein in trans. The rVHSV-P2 and -P3 were not generated from cells expressing truncated P proteins (P1, P2 or P3 protein), but the rVHSV-P1 produced infectious viruses, even in cells without any P-protein-expressing plasmids. Nucleotide sequence analysis of the P gene of rVHSV-P1 showed that a mutation had occurred that resulted in the fourth amino acid (isoleucine, ATT) being changed to methionine (ATG) without a frameshift (P0.5), suggesting that strong selection pressure might facilitate mutations that are advantageous or essential for virus replication. Infectious rVHSV-P2 and -P3 were produced in cells expressing the P0.5 protein, suggesting that the first three amino acids of the P protein of VHSV are dispensable for viral replication. Furthermore, although the P1 protein was shorter than the P0.5 protein by only two amino acid residues, no viruses were produced when the P1 protein was supplied indicating that the fourth and the fifth amino acid residues are indispensable for normal P protein functions involved in viral replication.
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PMID:Effect of truncation of the N-terminal region of the viral hemorrhagic septicemia virus (VHSV) P protein on viral replication. 2627 Nov 53