The Rhizobium etli CE3 O antigen is a fixed-length heteropolymer with O methylation being the predominant type of sugar modification. There are two O-methylated residues that occur, on average, once per complete O antigen: a multiply O-methylated terminal fucose and 2-O methylation of a fucose residue within a repeating unit. The amount of the methylated terminal fucose decreases and the amount of 2-O-methylfucose increases when bacteria are grown in the presence of the host plant, Phaseolus vulgaris, or its seed exudates. Insertion mutagenesis was used to identify open reading frames required for the presence of these O-methylated residues. The presence of the methylated terminal fucose required genes wreA, wreB, wreC, wreD, and wreF, whereas 2-O methylation of internal fucoses required the methyltransferase domain of bifunctional gene wreM. Mutants lacking only the methylated terminal fucose, lacking only 2-O methylation, or lacking both the methylated terminal fucose and 2-O methylation exhibited no other lipopolysaccharide structural defects. Thus, neither of these decorations is required for normal O-antigen length, transport, or assembly into the final lipopolysaccharide. This is in contrast to certain enteric bacteria in which the absence of a terminal decoration severely affects O-antigen length and transport. R. etli mutants lacking only the methylated terminal fucose were not altered in symbiosis with host Phaseolus vulgaris, whereas mutants lacking only 2-O-methylfucose exhibited a delay in nodule development during symbiosis. These results support previous conclusions that the methylated terminal fucose is dispensable for symbiosis, whereas 2-O methylation of internal fucoses somehow facilitates early events in symbiosis.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2812443 | PMC |
http://dx.doi.org/10.1128/JB.01154-09 | DOI Listing |
J Vector Borne Dis
January 2025
Department of Zoology, Faculty of Science, University of Jaffna, Jaffna, Sri Lanka.
Background And Objectives: Salivary glands proteins but not glycoconjugates have been previously studied in mosquito vectors of human diseases. Glycoconjugates from salivary gland-derived proteins from human-feeding tick vectors can elicit hypersensitivity reactions which may also occur with mosquito bites. Protein glycoconjugate in salivary glands of the principal arboviral vector Aedes aegypti and the rapidly spreading malaria vector Anopheles stephensi were therefore investigated.
View Article and Find Full Text PDFSpectrochim Acta A Mol Biomol Spectrosc
December 2024
Department of Chemistry, Indian Institute of Technology Roorkee, Roorkee 247667, Uttarakhand, India. Electronic address:
Sialic acid, a negatively charged nine-carbon monosaccharide, is mainly located at the terminal end of glycan chains on glycoproteins and glycolipids of cell surface and most secreted proteins. Elevated levels of sialylated glycans have been known as a hallmark in numerous cancers. As a result, sialic acid acts as a useful and accessible cancer biomarker for early cancer detection and monitoring the disease development during cancer treatment which is crucial in elevating the survival rate.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
School of Pharmacy, Guangdong Pharmaceutical University, Guangzhou, 510006, China. Electronic address:
Ganoderma lucidum spores are tiny mature germ cells ejected from the abaxial side of the pileus and were responsible for multiple pharmacological properties. The defatted G. lucidum spores are the byproducts after the extraction of G.
View Article and Find Full Text PDFJ Med Chem
November 2024
Dipartimento di Chimica, Università degli Studi di Milano, 20133 Milano, Italy.
bioRxiv
October 2024
Center for Tropical and Emerging Global Diseases, University of Georgia, Athens GA.
Cellular adaptations to change often involve post-translational modifications of nuclear and cytoplasmic proteins. An example found in protists and plants is the modification of serine and threonine residues of dozens to hundreds of nucleocytoplasmic proteins with a single fucose (O-Fuc). A nucleocytoplasmic O-fucosyltransferase (OFT) occurs in the pathogen , the social amoeba , and higher plants, where it is called Spy because mutants have a spindly appearance.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!