Honors Program


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Al-Sammak, Fatima. Characterizing Chlorovirus Glycosyltransferase A111/114R and Its Role in Major Capsid Protein Glycosylation. Undergraduate Honors Thesis. University of Nebraska-Lincoln. 2022.


Copyright Fatima Al-Sammak 2022.


Vp54 is a major capsid protein found in the prototype chlorovirus Paramecium bursaria chlorella virus 1 (PBCV-1). This major capsid protein contains a conserved glycan structure that is also found in other chloroviruses. The conserved glycan structure is made up of five sugars, and structural and in silico analyses indicate that the PBCV-1 encoded gene a111/114r is a glycosyltransferase responsible for attaching three of these sugars to the core glycan structure. This study utilized various cloning methods to examine the characteristics and role of the conserved glycosyltransferase A111/114R. This study is part of a research project, which has been published, entitled “Chlorovirus PBCV-1 Multidomain Protein A111/111R Has Three Glycosyltransferase Functions Involved in the Synthesis of Atypical N-Glycans” by Eric Noel, Anna Notaro, Immacolata Speciale, Garry Duncan, Cristina De Castro, and James Van Etten in 2021. I was acknowledged on the paper. This study, through various experimental methods including protein cloning, protein expression, and Glo AssaysTM, found strong evidence suggesting that each of the three domains of A111/114R is responsible for adding one of the three sugars to the core glycan structure. Domain one is a galactosyltransferase, domain two is a xylosyltransferase, and domain three is fucosyltransferase.