scholarly journals Versatility and Differential Roles of Cysteine Residues in Human Prostacyclin Receptor Structure and Function

2006 ◽  
Vol 281 (48) ◽  
pp. 37227-37236 ◽  
Author(s):  
Jeremiah Stitham ◽  
Scott R. Gleim ◽  
Karen Douville ◽  
Eric Arehart ◽  
John Hwa
2007 ◽  
Vol 82 (1-4) ◽  
pp. 95-108 ◽  
Author(s):  
Jeremiah Stitham ◽  
Eric J. Arehart ◽  
Scott R. Gleim ◽  
Karen L. Douville ◽  
John Hwa

2010 ◽  
Vol 2010 ◽  
pp. 1-10 ◽  
Author(s):  
J. Santiago Mejia ◽  
Erik N. Arthun ◽  
Richard G. Titus

One approach to identify epitopes that could be used in the design of vaccines to control several arthropod-borne diseases simultaneously is to look for common structural features in the secretome of the pathogens that cause them. Using a novel bioinformatics technique, cysteine-abundance and distribution analysis, we found that many different proteins secreted by several arthropod-borne pathogens, includingPlasmodium falciparum, Borrelia burgdorferi, and eight species of Proteobacteria, are devoid of cysteine residues. The identification of three cysteine-abundance and distribution patterns in several families of proteins secreted by pathogenic and nonpathogenic Proteobacteria, and not found when the amino acid analyzed was tryptophan, provides evidence of forces restricting the content of cysteine residues in microbial proteins during evolution. We discuss these findings in the context of protein structure and function, antigenicity and immunogenicity, and host-parasite relationships.


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