Suggestive Evidence for Darwinian Selection against Asparagine-Linked Glycans of Plasmodium falciparum and Toxoplasma gondii

Author:

Bushkin G. Guy1,Ratner Daniel M.1,Cui Jike1,Banerjee Sulagna1,Duraisingh Manoj T.2,Jennings Cameron V.2,Dvorin Jeffrey D.2,Gubbels Marc-Jan3,Robertson Seth D.3,Steffen Martin4,O'Keefe Barry R.5,Robbins Phillips W.1,Samuelson John1

Affiliation:

1. Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts 02118;

2. Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 02115;

3. Department of Biology, Boston College, Chestnut Hill, Massachusetts 02467;

4. Department of Pathology and Laboratory Medicine, Boston University Medical School, Boston, Massachusetts 02118; and

5. Molecular Targets Development Program, Center for Cancer Research, NCI-Frederick, Frederick, Maryland 21702

Abstract

ABSTRACT We are interested in asparagine-linked glycans (N-glycans) of Plasmodium falciparum and Toxoplasma gondii , because their N-glycan structures have been controversial and because we hypothesize that there might be selection against N-glycans in nucleus-encoded proteins that must pass through the endoplasmic reticulum (ER) prior to threading into the apicoplast. In support of our hypothesis, we observed the following. First, in protists with apicoplasts, there is extensive secondary loss of Alg enzymes that make lipid-linked precursors to N-glycans. Theileria makes no N-glycans, and Plasmodium makes a severely truncated N-glycan precursor composed of one or two GlcNAc residues. Second, secreted proteins of Toxoplasma , which uses its own 10-sugar precursor (Glc 3 Man 5 GlcNAc 2 ) and the host 14-sugar precursor (Glc 3 Man 9 GlcNAc 2 ) to make N-glycans, have very few sites for N glycosylation, and there is additional selection against N-glycan sites in its apicoplast-targeted proteins. Third, while the GlcNAc-binding Griffonia simplicifolia lectin II labels ER, rhoptries, and surface of plasmodia, there is no apicoplast labeling. Similarly, the antiretroviral lectin cyanovirin-N, which binds to N-glycans of Toxoplasma , labels ER and rhoptries, but there is no apicoplast labeling. We conclude that possible selection against N-glycans in protists with apicoplasts occurs by eliminating N-glycans ( Theileria ), reducing their length ( Plasmodium ), or reducing the number of N-glycan sites ( Toxoplasma ). In addition, occupation of N-glycan sites is markedly reduced in apicoplast proteins versus some secretory proteins in both Plasmodium and Toxoplasma .

Publisher

American Society for Microbiology

Subject

Molecular Biology,General Medicine,Microbiology

Reference59 articles.

1. Complete genome sequence of the apicomplexan, Cryptosporidium parvum;Abrahamsen M. S.;Science,2004

2. Oligosaccharide and glycoprotein microarrays as tools in HIV glycobiology; glycan-dependent gp120/protein interactions;Adams E. W.;Chem. Biol.,2004

3. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

4. PlasmoDB: a functional genomic database for malaria parasites;Aurrecoechea C.;Nucleic Acids Res.,2009

5. Evolution of quality control of protein-folding in the ER lumen;Banerjee S.;Proc. Natl. Acad. Sci. U. S. A.,2007

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