Phillips Wesley Robbins, PhD
Professor
Boston University Henry M. Goldman School of Dental Medicine
Dept of Molecular & Cell Biology

PhD, University of Illinois



Expertise in Chitin Synthesis:

In Saccharomyces cerevisiae most chitin is synthesized by Chs3p, which deposits chitin in the lateral cell wall and in the bud-neck region during cell division. We have recently found that addition of glucosamine (GlcN) to the growth medium leads to a three- to fourfold increase in cell wall chitin levels. We compared this result to the increases in cellular chitin levels associated with cell wall stress and with treatment of yeast with mating pheromone. Since all three phenomena lead to increases in precursors of chitin, we hypothesized that chitin synthesis is at least in part directly regulated by the size of this pool. This hypothesis was strengthened by our finding that addition of GlcN to the growth medium causes a rapid increase in chitin synthesis without any pronounced change in the expression of more than 6,000 genes monitored with Affymetrix gene expression chips. In other studies we found that the specific activity of Chs3p is higher in the total membrane fractions from cells grown in GlcN and from mutants with weakened cell walls. Sucrose gradient analysis shows that Chs3p is present in an inactive form in what may be Golgi compartments but as an active enzyme in other intracellular membrane-bound vesicles, as well as in the plasma membrane. We conclude that Chs3p-dependent chitin synthesis in S. cerevisiae is regulated both by the levels of intermediates of the UDP-GlcNAc biosynthetic pathway and by an increase in the activity of the enzyme in the plasma membrane.

Expertise in N-Linked Glycosylation in Protists (collaboration with John Samuelson):

The vast majority of eukaryotes (fungi, plants, animals, slime mold, and euglena) synthesize Asn-linked glycans (Alg) by means of a lipid-linked precursor dolichol-PP-GlcNAc2Man9Glc3. Knowledge of this pathway is important because defects in the glycosyltransferases (Alg1-Alg12 and others not yet identified), which make dolichol-PP-glycans, lead to numerous congenital disorders of glycosylation. We used bioinformatics and experimental methods to characterize Alg glycosyltransferases and dolichol-PP-glycans of diverse protists, including many human pathogens, with the following major conclusions. First, it is demonstrated that common ancestry is a useful method of predicting the Alg glycosyltransferase inventory of each eukaryote. Second, in the vast majority of cases, this inventory accurately predicts the dolichol-PP-glycans observed. Third, Alg glycosyltransferases are missing in sets from each organism (e.g., all of the glycosyltransferases that add glucose and mannose are absent from Giardia and Plasmodium). Fourth, dolichol-PP-GlcNAc2Man5 (present in Entamoeba and Trichomonas) and dolichol-PP- and N-linked GlcNAc2 (present in Giardia) have not been identified previously in wild-type organisms. Finally, the present diversity of protist and fungal dolichol-PP-linked glycans appears to result from secondary loss of glycosyltransferases from a common ancestor that contained the complete set of Alg glycosyltransferases.

Graduate Faculty (Primary Mentor of Grad Students)
Boston University School of Medicine, Division of Graduate Medical Sciences




Novel Broad Spectrum Therapeutic Glycans against Category B Pathogens
09/01/2010 - 08/31/2012 (PI)
Trustees of Boston College NIH NIAID
7U01AI075563-04

Three Lectin Model of Amebic Encystation and Excystation
01/01/2000 - 12/31/2002 (PI)
Harvard University NIH NIAID

Expression and Characterization of a Fourth Chitinase from the Fungal Pathogen Candida albicans
06/01/2000 - 05/31/2001 (Dept Sponsor)
American Association for Dental Research (AADR)




Yr Title Project-Sub Proj Pubs
2016 Biosecurity Core 2UC7AI095321-03-8666 1
2010 ROBBINS Glycosylation and Glycosidases-Cell and Molecular Biology 5R01GM031318-47 98
2009 ROBBINS Glycosylation and Glycosidases-Cell and Molecular Biology 5R01GM031318-46 98
2008 ANALYSIS OF FISSION YEAST CELL WALL 5P41RR010888-12-5229 236
2008 EVOLUTION AND DIVERSITY OF EUKARYOTIC GLYCOSYLATION 5P41RR010888-12-5253 236
2008 ROBBINS Glycosylation and Glycosidases-Cell and Molecular Biology 2R01GM031318-45A1 98
2007 ANALYSIS OF FISSION YEAST CELL WALL 2P41RR010888-11-8050 236
2007 EVOLUTION AND DIVERSITY OF EUKARYOTIC GLYCOSYLATION 2P41RR010888-11-8074 236
2007 Glycosylation and Glycosidases-Cell &Molecular Biology 3R01GM031318-44S1 98
2006 ANALYSIS OF FISSION YEAST CELL WALL 5P41RR010888-10-7146 236
Showing 10 of 36 results. Show All Results
Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.

  1. Bandini G, Haserick JR, Motari E, Ouologuem DT, Lourido S, Roos DS, Costello CE, Robbins PW, Samuelson J. O-fucosylated glycoproteins form assemblies in close proximity to the nuclear pore complexes of Toxoplasma gondii. Proc Natl Acad Sci U S A. 2016 Oct 11; 113(41):11567-11572.View Related Profiles. PMID: 27663739.
  2. Chatterjee A, Ratner DM, Ryan CM, Johnson PJ, O'Keefe BR, Secor WE, Anderson DJ, Robbins PW, Samuelson J. Anti-Retroviral Lectins Have Modest Effects on Adherence of Trichomonas vaginalis to Epithelial Cells In Vitro and on Recovery of Tritrichomonas foetus in a Mouse Vaginal Model. PLoS One. 2015; 10(8):e0135340.View Related Profiles. PMID: 26252012; PMCID: PMC4529277; DOI: 10.1371/journal.pone.0135340;.
  3. Samuelson J, Robbins PW. Effects of N-glycan precursor length diversity on quality control of protein folding and on protein glycosylation. Semin Cell Dev Biol. 2015 May; 41:121-8.View Related Profiles. PMID: 25475176; PMCID: PMC4452448; DOI: 10.1016/j.semcdb.2014.11.008;.
  4. Samuelson J, Bushkin GG, Chatterjee A, Robbins PW. Strategies to discover the structural components of cyst and oocyst walls. Eukaryot Cell. 2013 Dec; 12(12):1578-87.View Related Profiles. PMID: 24096907; PMCID: PMC3889564; DOI: 10.1128/EC.00213-13;.
  5. Bushkin GG, Motari E, Carpentieri A, Dubey JP, Costello CE, Robbins PW, Samuelson J. Evidence for a structural role for acid-fast lipids in oocyst walls of Cryptosporidium, Toxoplasma, and Eimeria. MBio. 2013; 4(5):e00387-13.View Related Profiles. PMID: 24003177; PMCID: PMC3760245; DOI: 10.1128/mBio.00387-13;.
  6. Bushkin GG, Motari E, Magnelli P, Gubbels MJ, Dubey JP, Miska KB, Bullitt E, Costello CE, Robbins PW, Samuelson J. ß-1,3-glucan, which can be targeted by drugs, forms a trabecular scaffold in the oocyst walls of Toxoplasma and Eimeria. MBio. 2012; 3(5).View Related Profiles. PMID: 23015739; PMCID: PMC3518913; DOI: 10.1128/mBio.00258-12;.
  7. Samuelson J, Robbins P. A simple fibril and lectin model for cyst walls of Entamoeba and perhaps Giardia. Trends Parasitol. 2011 Jan; 27(1):17-22.View Related Profiles. PMID: 20934911; PMCID: PMC3014499; DOI: 10.1016/j.pt.2010.09.002;.
  8. Robbins P. Stents, statins, and other dumb luck. J Biol Chem. 2011 Jan 21; 286(3):1669-74. PMID: 21098482; PMCID: PMC3023461; DOI: 10.1074/jbc.X110.205633;.
  9. Carpentieri A, Ratner DM, Ghosh SK, Banerjee S, Bushkin GG, Cui J, Lubrano M, Steffen M, Costello CE, O'Keefe B, Robbins PW, Samuelson J. The antiretroviral lectin cyanovirin-N targets well-known and novel targets on the surface of Entamoeba histolytica trophozoites. Eukaryot Cell. 2010 Nov; 9(11):1661-8.View Related Profiles. PMID: 20852023; PMCID: PMC2976296; DOI: 10.1128/EC.00166-10;.
  10. Chatterjee A, Carpentieri A, Ratner DM, Bullitt E, Costello CE, Robbins PW, Samuelson J. Giardia cyst wall protein 1 is a lectin that binds to curled fibrils of the GalNAc homopolymer. PLoS Pathog. 2010; 6(8):e1001059.View Related Profiles. PMID: 20808847; PMCID: PMC2924369; DOI: 10.1371/journal.ppat.1001059;.
Showing 10 of 113 results. Show More

This graph shows the total number of publications by year, by first, middle/unknown, or last author.

Bar chart showing 108 publications over 35 distinct years, with a maximum of 10 publications in 1996

YearPublications
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72 E. Concord St Evans Building
Boston MA 02118
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