Disease relevance of Chenopodium quinoa

• Biological assays conducted in Chenopodium quinoa (local lesion host) and Nicotiana benthamiana (systemic host) revealed that variants lacking either 12 N-proximal amino acids or a region containing four consecutive arginine residues of the CP N-terminus were competent for assembly into virions and remained infectious in plants [1].
• Spatio-temporal analysis of the RNAs, coat and movement (p7) proteins of Carnation mottle virus in Chenopodium quinoa plants [2].
• The RNA-dependent RNA polymerase (RdRp) of foxtail mosaic virus (FMV) was partially purified from infected leaves of Chenopodium quinoa [3].

High impact information on Chenopodium quinoa

• Precise replacement of the open reading frame with sequences encoding chloramphenicol acetyltransferase resulted in high level expression of chloramphenicol acetyltransferase in infected C. quinoa, indicating that satBaMV is potentially useful as a satellite-based expression vector [4].
• A remarkable covariation of eight site-specific amino acids was found in the HCRSV capsid protein (CP) after serial passages in C. quinoa: Val(49)-->Ile, Ile(95)-->Val, Lys(270)-->Arg, Gly(272)-->Asp, Tyr(274)-->His, Ala(311)-->Asp, Asp(334)-->Ala, and Ala(335)-->Thr [5].
• The virus produced from these constructs retained its ability to express BNYVV cp in local infections during successive passages on C. quinoa [6].
• Analysis of virion RNA for each B3 variant recovered from symptomatic leaves of Chenopodium quinoa revealed that the interactions between the N-terminal ARM of BMV CP and each of three genomic RNAs is distinct [7].
• Two isolates, S6 and NEP-1, infected C. quinoa systemically, but had a serine at position 47 of the CP [8].

Biological context of Chenopodium quinoa

• Glycemic index (GI) for GF pasta was similar to GI for GF bread while GI for quinoa was slightly lower than that of GF pasta and bread [9].

Associations of Chenopodium quinoa with chemical compounds

• Two isolates that infected C. quinoa systemically had a proline at position 47 [8].
• The alfalfa hederagenin saponin and Quinoa also formed pore-sheets, despite lacking adjuvanticity [10].
• In addition, triglyceride concentrations were significantly reduced for quinoa with respect to GF bread and bread [9].
• Identification and biological activities of triterpenoid saponins from Chenopodium quinoa [11].
• Two flavonol glycosides from Chenopodium quinoa [12].

Gene context of Chenopodium quinoa

• In contrast to these observations in C. quinoa, none of the CP variants was able to establish either local or systemic infections in barley plants [13].
• Tissue-prints and time course experiments on infected C. quinoa plants confirmed that P38 is present at a high level late in infection and is a final maturation product of the GFLV RNA2 polyprotein in vivo [14].
• The AUCs of digested starch of quinoa and the two samples of pasta were not statistically different [9].
• Soluble carbohydrate levels and invertase, sucrose synthase (SS), sucrose-6-phosphate synthase (SPS) and alpha-amylase activities were analysed in cotyledons and embryonic axes of quinoa seedlings grown at 5 degrees C and 25 degrees C in the dark [15].
• The results showed that p25 was present as a soluble protein only in the S30 fraction of T. expansa, C. quinoa and sugarbeet leaves infected with BNYVV [16].

Analytical, diagnostic and therapeutic context of Chenopodium quinoa

• When partially purified extracts were subjected to sucrose density gradient centrifugation, infectivity on C. quinoa from certain 2-fraction combinations was higher than expected, compared to the infectivity of the individual fractions [17].

References