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MeSH Review

Chenopodium quinoa

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Disease relevance of Chenopodium quinoa


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


Associations of Chenopodium quinoa with chemical compounds


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].


  1. Deletions in the conserved amino-terminal basic arm of cucumber mosaic virus coat protein disrupt virion assembly but do not abolish infectivity and cell-to-cell movement. Schmitz, I., Rao, A.L. Virology (1998) [Pubmed]
  2. Spatio-temporal analysis of the RNAs, coat and movement (p7) proteins of Carnation mottle virus in Chenopodium quinoa plants. García-Castillo, S., Sánchez-Pina, M.A., Pallás, V. J. Gen. Virol. (2003) [Pubmed]
  3. Partial purification and characterization of foxtail mosaic potexvirus RNA-dependent RNA polymerase. Rouleau, M., Bancroft, J.B., Mackie, G.A. Virology (1993) [Pubmed]
  4. The open reading frame of bamboo mosaic potexvirus satellite RNA is not essential for its replication and can be replaced with a bacterial gene. Lin, N.S., Lee, Y.S., Lin, B.Y., Lee, C.W., Hsu, Y.H. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  5. Covariation in the capsid protein of hibiscus chlorotic ringspot virus induced by serial passaging in a host that restricts movement leads to avirulence in its systemic host. Liang, X.Z., Lee, B.T., Wong, S.M. J. Virol. (2002) [Pubmed]
  6. Zygocactus virus X-based expression vectors and formation of rod-shaped virus-like particles in plants by the expressed coat proteins of Beet necrotic yellow vein virus and Soil-borne cereal mosaic virus. Koenig, R., Lesemann, D.E., Loss, S., Engelmann, J., Commandeur, U., Deml, G., Schiemann, J., Aust, H., Burgermeister, W. J. Gen. Virol. (2006) [Pubmed]
  7. Molecular studies on bromovirus capsid protein. Choi, Y.G., Grantham, G.L., Rao, A.L. Virology (2000) [Pubmed]
  8. A single conserved amino acid in the coat protein gene of pea seed-borne mosaic potyvirus modulates the ability of the virus to move systemically in Chenopodium quinoa. Andersen, K., Johansen, I.E. Virology (1998) [Pubmed]
  9. In vitro starch digestibility and in vivo glucose response of gluten-free foods and their gluten counterparts. Berti, C., Riso, P., Monti, L.D., Porrini, M. European journal of nutrition. (2004) [Pubmed]
  10. Adjuvanticity and ISCOM formation by structurally diverse saponins. Bomford, R., Stapleton, M., Winsor, S., Beesley, J.E., Jessup, E.A., Price, K.R., Fenwick, G.R. Vaccine (1992) [Pubmed]
  11. Identification and biological activities of triterpenoid saponins from Chenopodium quinoa. Woldemichael, G.M., Wink, M. J. Agric. Food Chem. (2001) [Pubmed]
  12. Two flavonol glycosides from Chenopodium quinoa. De Simone, F., Dini, A., Pizza, C., Saturnino, P., Schettino, O. Phytochemistry (1990) [Pubmed]
  13. Molecular studies on bromovirus capsid protein. II. Functional analysis of the amino-terminal arginine-rich motif and its role in encapsidation, movement, and pathology. Rao, A.L., Grantham, G.L. Virology (1996) [Pubmed]
  14. Grapevine fanleaf nepovirus P38 putative movement protein is not transiently expressed and is a stable final maturation product in vivo. Ritzenthaler, C., Pinck, M., Pinck, L. J. Gen. Virol. (1995) [Pubmed]
  15. Changes in soluble carbohydrates and related enzymes induced by low temperature during early developmental stages of quinoa (Chenopodium quinoa) seedlings. Rosa, M., Hilal, M., González, J.A., Prado, F.E. J. Plant Physiol. (2004) [Pubmed]
  16. Immunodetection of beet necrotic yellow vein virus RNA3-encoded protein in different host plants and tissues. Li, Y., Wei, C., Tien, P., Pan, N., Chen, Z. Acta Virol. (1996) [Pubmed]
  17. Citrus psorosis is probably caused by a bipartite ssRNA virus. Garcia, M.L., Grau, O., Sarachu, A.N. Res. Virol. (1991) [Pubmed]
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