Plants of the golden Camellia group are not only high-quality camellia germplasm , but also a plant group with rich medicinal and nutritional value, which are used as food, cosmetics and traditional medicine in China. There are approximately 50 species in this group around the world, and more than 30 species of golden camelliaplants have been published in China. The leaves and flowers of these species have similar shapes, so they are often confused as species. Our study used simplified genome sequencing technology to construct a phylogenetic tree of plants in the Chinese golden Camellia group and describe the evolutionary relationships . At the same time, the secondary metabolic indexes of total phenols, total flavonoids, total anthocyanins and ellagic acid in the leaves were determined., and principal component clustering analysis was performed . The results showed that the chemical classification and genetic phylogenetic trees showed some of the same trends, indicating that Camellia chinensis can be used as Biomarkers for chemical type. The research results provide phylogenetic information for the genotype and performance diversity of golden camelliaregionally distributed in China. At the same time, molecular biology phylogenetic methods are used to understand or explain the characteristics of secondary metabolites of golden Camellia , and provide theoretical basis for the search and development of potential bioactive substances.

Antibodies are important tools for the study of membrane proteins in biological, biophysics and structural analyses. However, the production of purified membrane proteins is still a formidable challenge due to the amphipathic character and inherent instability of these proteins. In this work, we tested a strategy for producing antibodies against an ATP-Binding Cassette (ABC) transporter without the need to produce the full membrane complex. Instead, just the extra cytoplasmic regions of the ABC-type transporter Rv1819c from Mycobacterium tuberculosis were presented in the RAD-display, a scaffold system based on the engineered Pyrococcus furiosus RadA protein developed for exposition of peptides. The RadA scaffold protein is highly stable, can tolerate long insertions and easy to produce in Escherichia coli. Based on the three-dimensional structure of Rv1891c, we selected two versions of the main extracellular loops of the permease to use as test cases for this approach. Rv1819c-derived peptides displayed on RAD display system were used for immunization of mice and production of polyclonal antibodies. These antibodies were able to recognize the transporter in M. tuberculosis cell extracts, on intact cells by flow cytometry and as purified protein. The results showed the approach can be a useful tool for in vitro analyses, screening, and evaluation of different epitopes in membrane proteins.