scholarly journals Comparative Analysis Of Amino Acid Sequence Diversity And Physiochemical Properties Of Peroxidase Superfamily

2020 ◽  
Vol 2 (1) ◽  
pp. 1-8
Author(s):  
Shamsher S Kanwar ◽  
1983 ◽  
Vol 158 (5) ◽  
pp. 1615-1634 ◽  
Author(s):  
C A Slaughter ◽  
J D Capra

VH region amino acid sequences are described for five A/J anti-p-azophenylarsonate (anti-Ars) hybridoma antibodies for which the VL region sequences have previously been determined, thus completing the V domain sequences of these molecules. These antibodies all belong to the family designated Ars-A which bears the major anti-arsonate cross-reactive idiotype (CRI) of the A strain mouse. However, they differ in the degree to which they express the CRI in standard competition radioimmunoassays. Although the sequences are closely related, all are different from each other. Replacements are distributed throughout the VH region and occur in positions of the chain encoded by all three gene segments, VH, DH, and JH. It is likely that somatic diversification processes play a dominant role in producing the sequence variability in each of these segments. The number of differences from the sequence encoded by the germline is smallest for antibodies that express the CRI most strongly, suggesting that somatic diversification is responsible for loss of the CRI in members of the Ars-A antibody family. There is an unusual degree of clustering of differences in both CDR2 and CDR3 and many of the substitutions are located in "hot spots" of variation. The large number of differences between the chains prohibits the unambiguous identification of positions at which alterations play a major role in reducing the expression of the CRI. However, the data suggest that the loss of the CRI is associated with a definable repertoire of somatic changes at a restricted number of highly variable sites.


1998 ◽  
Vol 112 (2) ◽  
pp. 146-152 ◽  
Author(s):  
J.Michael Conlon ◽  
James E. Platz ◽  
Nicolas Chartrel ◽  
Hubert Vaudry ◽  
Per F. Nielsen

2019 ◽  
Vol 4 (Suppl 3) ◽  
pp. A61.3-A62
Author(s):  
Roland Funwei ◽  
Catherine O Falade ◽  
Olusola Ojurongbe

BackgroundPrompt diagnosis and appropriate treatment remain the hallmark needed to reduce malaria-related mortality in areas of high transmission. Rapid diagnostic tests (RDTs) that target the Pfhrp-2 gene, are essential in resource-limited settings where microscopy is not available. However, Pfhrp-2 gene deletion is implicated in limiting RDT sensitivity. Studies evaluating Pfhrp-2 and Pfhrp-3 deletion and the amino acid sequence diversity has not been investigated in Nigeria. We therefore hypothesised that malaria parasites in Nigeria are lacking Pfhrp-2/Pfhrp-3 genes with variable amino acid repeats sequences.MethodsThe study was part of a prospective cohort study evaluating RDTs performance. We pooled 66 samples comprising false negatives (n=31) and true positives (n=35) to elucidate Pfhrp-2/Pfhrp-3 gene deletion, RDT cross-reactivity with Pfhrp-3 antigen and amino acid sequence diversity. The 18SrRNA, msp 1, msp2 and glurp genes were amplified to establish active Plasmodium falciparum infection and the exon-2 regions of Pfhrp-2 and Pfhrp-3 genes were amplified to determine the presence or absence of Pfhrp-2 and Pfhrp-3 genes. Isolates with conserved Pfhrp-2/Pfhrp-3 were sequenced.ResultsAll 66 samples were positive for 18SrRNA, msp1, msp2 and glurp, indicating active P. falciparum infection. However, 16.7% and 6.0% of the samples were lacking Pfhrp-2 and Pfhrp-3 genes. Of the false negative samples, 25.8% and 12.9% has Pfhrp-2 and Pfhrp-3 deletions. Three Pfhrp-3 conserved antigens cross reacted to give RDT positive results. An extensive diversity in the amino acid sequence was observed.ConclusionPlasmodium falciparum parasites in Nigeria lack Pfhrp-2 and Pfhrp-3 genes. However, the proportion of deletions is low compared to reports from other malaria-endemic regions. In addition, a high amino acid tandem repeat was observed. A combination of pLDH and Pfhrp-2 based RDTs is recommended for accurate malaria diagnosis.


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