Common, Intermediate and Well-Documented HLA Alleles in World Populations: CIWD Version 3.0.0

A catalog of common, intermediate and well-documented (CIWD) HLA-A, -B, -C, -DRB1, -DRB3, -DRB4, -DRB5, -DQB1 and -DPB1 alleles has been compiled from over 8 million individuals using data from 20 unrelated hematopoietic stem cell volunteer donor registries. Individuals are divided into seven geographic/ancestral/ethnic groups and data are summarized for each group and for the total population. P (two-field) and G group assignments are divided into one of four frequency categories: common (≥1 in 10 000), intermediate (≥1 in 100 000), well-documented (≥5 occurrences) or not-CIWD. Overall 26% of alleles in IPD-IMGT/HLA version 3.31.0 at P group resolution fall into the three CIWD categories. The two-field catalog includes 18% (n = 545) common, 17% (n = 513) intermediate, and 65% (n = 1997) well-documented alleles. Full-field allele frequency data are provided but are limited in value by the variations in resolution used by the registries. A recommended CIWD list is based on the most frequent category in the total or any of the seven geographic/ancestral/ethnic groups. Data are also provided so users can compile a catalog specific to the population groups that they serve. Comparisons are made to three previous CWD reports representing more limited population groups. This catalog, CIWD version 3.0.0, is a step closer to the collection of global HLA frequencies and to a clearer view of HLA diversity in the human population as a whole

Investigation of E2 protein surface charge to facilitate drug delivery.

The physical characterization of the nanoparticles and their surface can be used to assess binding interactions with cells in biological conditions. The surface properties of E2 protein, a self-assembled protein cage, have not been investigated thoroughly. This study investigates the effect of pH and ionic strength on the surface charge of E2 protein using zeta potential. E2 protein, a subunit of the pyruvate dehydrogenase multienzyme complex, was produced in Escherichia coli (BL21 (DE3)). E2 protein has been found to be a negatively charged protein. The isoelectric point of E2 is found to be around 3.5 after it was suspended in 50 mM sodium phosphate buffer between pH 3 to pH 10. The hydrodynamic diameter of E2 when suspended in the different pH level was found to be very stable except in the region between pH 3 and pH 4, where agglomeration was observed. The decrease in zeta potential of E2 protein in 0M NaCl solution was observed and concluded that the protein retains optimum colloidal stability in this solution.Bachelor of Engineering (Chemical and Biomolecular Engineering