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Journal articles on the topic 'CMP-sialic acid synthetases'

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Published: 4 June 2021

Last updated: 19 February 2023

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1

Münster, Anja-K., Matthias Eckhardt, Barry Potvin, Martina Mühlenhoff, Pamela Stanley, and Rita Gerardy-Schahn. "Mammalian cytidine 5′-monophosphateN-acetylneuraminic acid synthetase: A nuclear protein with evolutionarily conserved structural motifs." Proceedings of the National Academy of Sciences 95, no. 16 (August 4, 1998): 9140–45. http://dx.doi.org/10.1073/pnas.95.16.9140.

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Sialic acids of cell surface glycoproteins and glycolipids play a pivotal role in the structure and function of animal tissues. The pattern of cell surface sialylation is species- and tissue-specific, is highly regulated during embryonic development, and changes with stages of differentiation. A prerequisite for the synthesis of sialylated glycoconjugates is the activated sugar-nucleotide cytidine 5′-monophosphateN-acetylneuraminic acid (CMP-Neu5Ac), which provides a substrate for Golgi sialyltransferases. Although a mammalian enzymatic activity responsible for the synthesis of CMP-Neu5Ac has been described and the enzyme has been purified to near homogeneity, sequence information is restricted to bacterial CMP-Neu5Ac synthetases. In this paper, we describe the molecular characterization, functional expression, and subcellular localization of murine CMP-Neu5Ac synthetase. Cloning was achieved by complementation of the Chinese hamster ovarylec32mutation that causes a deficiency in CMP-Neu5Ac synthetase activity. A murine cDNA encoding a protein of 432 amino acids rescued thelec32mutation and also caused polysialic acid to be expressed in the capsule of the CMP-Neu5Ac synthetase negativeEscherichia colimutant EV5. Three potential nuclear localization signals were found in the murine synthetase, and immunofluorescence studies confirmed predominantly nuclear localization of an N-terminally Flag-tagged molecule. Four stretches of amino acids that occur in the N-terminal region are highly conserved in bacterial CMP-Neu5Ac synthetases, providing evidence for an ancestral relationship between the sialylation pathways of bacterial and animal cells.

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2

Munster-Kuhnel, A. K. "Structure and function of vertebrate CMP-sialic acid synthetases." Glycobiology 14, no. 10 (May 26, 2004): 43R—51R. http://dx.doi.org/10.1093/glycob/cwh113.

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3

Schaper, Wiebke, Joachim Bentrop, Jana Ustinova, Linda Blume, Elina Kats, Joe Tiralongo, Birgit Weinhold, Martin Bastmeyer, and Anja-K. Münster-Kühnel. "Identification and Biochemical Characterization of Two Functional CMP-Sialic Acid Synthetases inDanio rerio." Journal of Biological Chemistry 287, no. 16 (February 20, 2012): 13239–48. http://dx.doi.org/10.1074/jbc.m111.327544.

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4

Yu, Hai, Hui Yu, Rebekah Karpel, and Xi Chen. "Chemoenzymatic synthesis of CMP–sialic acid derivatives by a one-pot two-enzyme system: comparison of substrate flexibility of three microbial CMP–sialic acid synthetases." Bioorganic & Medicinal Chemistry 12, no. 24 (December 2004): 6427–35. http://dx.doi.org/10.1016/j.bmc.2004.09.030.

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5

Oschlies, Melanie, Achim Dickmanns, Thomas Haselhorst, Wiebke Schaper, Katharina Stummeyer, Joe Tiralongo, Birgit Weinhold, et al. "A C-Terminal Phosphatase Module Conserved in Vertebrate CMP-Sialic Acid Synthetases Provides a Tetramerization Interface for the Physiologically Active Enzyme." Journal of Molecular Biology 393, no. 1 (October 2009): 83–97. http://dx.doi.org/10.1016/j.jmb.2009.08.003.

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6

Yu, Hai, Jie Zeng, Yanhong Li, Vireak Thon, Baojun Shi, and Xi Chen. "Effective one-pot multienzyme (OPME) synthesis of monotreme milk oligosaccharides and other sialosides containing 4-O-acetyl sialic acid." Organic & Biomolecular Chemistry 14, no. 36 (2016): 8586–97. http://dx.doi.org/10.1039/c6ob01706a.

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Chemoenzymatic synthesis: Monotreme milk glycans and other sialosides containing a 4-O-acetyl-sialic acid were synthesized in a gram or preparative scales using a one-pot two-enzyme sialylation system containing bacterial CMP-sialic acid synthetase and sialyltransferase PmST3.

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7

KEAN, E. "CMP-sialic acid synthetase of the nucleus." Biochimica et Biophysica Acta (BBA) - General Subjects 1673, no. 1-2 (July 2004): 56–65. http://dx.doi.org/10.1016/j.bbagen.2004.04.006.

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8

STOUGHTON, Daniel M., Gerardo ZAPATA, Robert PICONE, and Willie F. VANN. "Identification of Arg-12 in the active site of Escherichia coli K1 CMP-sialic acid synthetase." Biochemical Journal 343, no. 2 (October 8, 1999): 397–402. http://dx.doi.org/10.1042/bj3430397.

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Escherichia coli K1 CMP-sialic acid synthetase catalyses the synthesis of CMP-sialic acid from CTP and sialic acid. The active site of the 418 amino acid E. coli enzyme was localized to its N-terminal half. The bacterial CMP-sialic acid synthetase enzymes have a conserved motif, IAIIPARXXSKGLXXKN, at their N-termini. Several basic residues have been identified at or near the active site of the E. coli enzyme by chemical modification and site-directed mutagenesis. Only one of the lysines in the N-terminal motif, Lys-21, appears to be essential for activity. Mutation of Lys-21 in the N-terminal motif results in an inactive enzyme. Furthermore, Arg-12 of the N-terminal motif appears to be an active-site residue, based on the following evidence. Substituting Arg-12 with glycine or alanine resulted in inactive enzymes, indicating that this residue is required for enzymic activity. The Arg-12 → Lys mutant was partially active, demonstrating that a positive charge is required at this site. Steady-state kinetic analysis reveals changes in kcat, Km and Ks for CTP, which implicates Arg-12 in catalysis and substrate binding.

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9

Bose, Sucharita, Debayan Purkait, Deepthi Joseph, Vinod Nayak, and Ramaswamy Subramanian. "Structural and functional characterization of CMP-N-acetylneuraminate synthetase fromVibrio cholerae." Acta Crystallographica Section D Structural Biology 75, no. 6 (May 31, 2019): 564–77. http://dx.doi.org/10.1107/s2059798319006831.

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Several pathogenic bacteria utilize sialic acid, including host-derivedN-acetylneuraminic acid (Neu5Ac), in at least two ways: they use it as a nutrient source and as a host-evasion strategy by coating themselves with Neu5Ac. Given the significant role of sialic acid in pathogenesis and host-gut colonization by various pathogenic bacteria, includingNeisseria meningitidis,Haemophilus influenzae,Pasteurella multocidaandVibrio cholerae, several enzymes of the sialic acid catabolic, biosynthetic and incorporation pathways are considered to be potential drug targets. In this work, findings on the structural and functional characterization of CMP-N-acetylneuraminate synthetase (CMAS), a key enzyme in the incorporation pathway, fromVibrio choleraeare reported. CMAS catalyzes the synthesis of CMP-sialic acid by utilizing CTP and sialic acid. Crystal structures of the apo and the CDP-bound forms of the enzyme were determined, which allowed the identification of the metal cofactor Mg2+in the active site interacting with CDP and the invariant Asp215 residue. While open and closed structural forms of the enzyme from eukaryotic and other bacterial species have already been characterized, a partially closed structure ofV. choleraeCMAS (VcCMAS) observed upon CDP binding, representing an intermediate state, is reported here. The kinetic data suggest that VcCMAS is capable of activating the two most common sialic acid derivatives, Neu5Ac and Neu5Gc. Amino-acid sequence and structural comparison of the active site of VcCMAS with those of eukaryotic and other bacterial counterparts reveal a diverse hydrophobic pocket that interacts with the C5 substituents of sialic acid. Analyses of the thermodynamic signatures obtained from the binding of the nucleotide (CTP) and the product (CMP-sialic acid) to VcCMAS provide fundamental information on the energetics of the binding process.

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10

Li, Yanhong, Hai Yu, Hongzhi Cao, Saddam Muthana, and Xi Chen. "Pasteurella multocida CMP-sialic acid synthetase and mutants of Neisseria meningitidis CMP-sialic acid synthetase with improved substrate promiscuity." Applied Microbiology and Biotechnology 93, no. 6 (October 4, 2011): 2411–23. http://dx.doi.org/10.1007/s00253-011-3579-6.

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11

Liu, Jennifer Lin Chun, Gwo Jenn Shen, Yoshitaka Ichikawa, James F. Rutan, Gerardo Zapata, Willie F. Vann, and Chi Huey Wong. "Overproduction of CMP-sialic acid synthetase for organic synthesis." Journal of the American Chemical Society 114, no. 10 (May 1992): 3901–10. http://dx.doi.org/10.1021/ja00036a044.

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12

Viswanathan, Karthik, Noboru Tomiya, Jung Park, Sundeep Singh, Yuan C. Lee, Karen Palter, and Michael J. Betenbaugh. "Expression of a Functional Drosophila melanogaster CMP-sialic Acid Synthetase." Journal of Biological Chemistry 281, no. 23 (March 14, 2006): 15929–40. http://dx.doi.org/10.1074/jbc.m512186200.

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13

Yu, Ching-Ching, Po-Chiao Lin, and Chun-Cheng Lin. "Site-specific immobilization of CMP-sialic acid synthetase on magnetic nanoparticles and its use in the synthesis of CMP-sialic acid." Chemical Communications, no. 11 (2008): 1308. http://dx.doi.org/10.1039/b716330d.

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14

Misaki, Ryo, Kazuhito Fujiyama, and Tatsuji Seki. "Expression of human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell." Biochemical and Biophysical Research Communications 339, no. 4 (January 2006): 1184–89. http://dx.doi.org/10.1016/j.bbrc.2005.11.130.

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15

Mertsalov, Ilya B., Boris N. Novikov, Hilary Scott, Lawrence Dangott, and Vladislav M. Panin. "Characterization of Drosophila CMP-sialic acid synthetase activity reveals unusual enzymatic properties." Biochemical Journal 473, no. 13 (June 28, 2016): 1905–16. http://dx.doi.org/10.1042/bcj20160347.

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DmCSAS has unique localization in the cell secretory compartment. Our results demonstrated that DmCSAS has unusual enzymatic properties that revealed evolutionary adaptation to the milieu of the Golgi compartment and suggested mechanisms that control sialylation in insect organisms.

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16

Lewis, Amanda L., Hongzhi Cao, Silpa K. Patel, Sandra Diaz, Wesley Ryan, Aaron F. Carlin, Vireak Thon, et al. "NeuA Sialic Acid O-Acetylesterase Activity Modulates O-Acetylation of Capsular Polysaccharide in Group B Streptococcus." Journal of Biological Chemistry 282, no. 38 (July 23, 2007): 27562–71. http://dx.doi.org/10.1074/jbc.m700340200.

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Group B Streptococcus (GBS) is a common cause of neonatal sepsis and meningitis. A major GBS virulence determinant is its sialic acid (Sia)-capped capsular polysaccharide. Recently, we discovered the presence and genetic basis of capsular Sia O-acetylation in GBS. We now characterize a GBS Sia O-acetylesterase that modulates the degree of GBS surface O-acetylation. The GBS Sia O-acetylesterase operates cooperatively with the GBS CMP-Sia synthetase, both part of a single polypeptide encoded by the neuA gene. NeuA de-O-acetylation of free 9-O-acetyl-N-acetylneuraminic acid (Neu5,9Ac2) was enhanced by CTP and Mg2+, the substrate and co-factor, respectively, of the N-terminal GBS CMP-Sia synthetase domain. In contrast, the homologous bifunctional NeuA esterase from Escherichia coli K1 did not display cofactor dependence. Further analyses showed that in vitro, GBS NeuA can operate via two alternate enzymatic pathways: de-O-acetylation of Neu5,9Ac2 followed by CMP activation of Neu5Ac or activation of Neu5,9Ac2 followed by de-O-acetylation of CMP-Neu5,9Ac2. Consistent with in vitro esterase assays, genetic deletion of GBS neuA led to accumulation of intracellular O-acetylated Sias, and overexpression of GBS NeuA reduced O-acetylation of Sias on the bacterial surface. Site-directed mutagenesis of conserved asparagine residue 301 abolished esterase activity but preserved CMP-Sia synthetase activity, as evidenced by hyper-O-acetylation of capsular polysaccharide Sias on GBS expressing only the N301A NeuA allele. These studies demonstrate a novel mechanism regulating the extent of capsular Sia O-acetylation in intact bacteria and provide a genetic strategy for manipulating GBS O-acetylation in order to explore the role of this modification in GBS pathogenesis and immunogenicity.

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17

Wong, Jessica H., Urvashi Sahni, Yanhong Li, Xi Chen, and Jacquelyn Gervay-Hague. "Synthesis of sulfone-based nucleotide isosteres: identification of CMP-sialic acid synthetase inhibitors." Org. Biomol. Chem. 7, no. 1 (2009): 27–29. http://dx.doi.org/10.1039/b819155g.

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18

Karwaski, Marie-France, Warren W. Wakarchuk, and Michel Gilbert. "High-level expression of recombinant Neisseria CMP-sialic acid synthetase in Escherichia coli." Protein Expression and Purification 25, no. 2 (July 2002): 237–40. http://dx.doi.org/10.1016/s1046-5928(02)00004-9.

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19

Urbanek, Kelly, Danica M. Sutherland, Robert C. Orchard, Craig B. Wilen, Jonathan J. Knowlton, Pavithra Aravamudhan, Gwen M. Taylor, Herbert W. Virgin, and Terence S. Dermody. "Cytidine Monophosphate N-Acetylneuraminic Acid Synthetase and Solute Carrier Family 35 Member A1 Are Required for Reovirus Binding and Infection." Journal of Virology 95, no. 2 (October 21, 2020): e01571-20. http://dx.doi.org/10.1128/jvi.01571-20.

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ABSTRACTEngagement of cell surface receptors by viruses is a critical determinant of viral tropism and disease. The reovirus attachment protein σ1 binds sialylated glycans and proteinaceous receptors to mediate infection, but the specific requirements for different cell types are not entirely known. To identify host factors required for reovirus-induced cell death, we conducted a CRISPR-knockout screen targeting over 20,000 genes in murine microglial BV2 cells. Candidate genes required for reovirus to cause cell death were highly enriched for sialic acid synthesis and transport. Two of the top candidates identified, CMP N-acetylneuraminic acid synthetase (Cmas) and solute carrier family 35 member A1 (Slc35a1), promote sialic acid expression on the cell surface. Two reovirus strains that differ in the capacity to bind sialic acid, T3SA+ and T3SA−, were used to evaluate Cmas and Slc35a1 as potential host genes required for reovirus infection. Following CRISPR-Cas9 disruption of either gene, cell surface expression of sialic acid was diminished. These results correlated with decreased binding of strain T3SA+, which is capable of engaging sialic acid. Disruption of either gene did not alter the low-level binding of T3SA−, which does not engage sialic acid. Furthermore, infectivity of T3SA+ was diminished to levels similar to those of T3SA− in cells lacking Cmas and Slc35a1 by CRISPR ablation. However, exogenous expression of Cmas and Slc35a1 into the respective null cells restored sialic acid expression and T3SA+ binding and infectivity. These results demonstrate that Cmas and Slc35a1, which mediate cell surface expression of sialic acid, are required in murine microglial cells for efficient reovirus binding and infection.IMPORTANCE Attachment factors and receptors are important determinants of dissemination and tropism during reovirus-induced disease. In a CRISPR cell survival screen, we discovered two genes, Cmas and Slc35a1, which encode proteins required for sialic acid expression on the cell surface and mediate reovirus infection of microglial cells. This work elucidates host genes that render microglial cells susceptible to reovirus infection and expands current understanding of the receptors on microglial cells that are engaged by reovirus. Such knowledge may lead to new strategies to selectively target microglial cells for oncolytic applications.

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20

Mosimann, Steven C., Michel Gilbert, Dennise Dombroswki, Rebecca To, Warren Wakarchuk, and Natalie C. J. Strynadka. "Structure of a Sialic Acid-activating Synthetase, CMP-acylneuraminate Synthetase in the Presence and Absence of CDP." Journal of Biological Chemistry 276, no. 11 (December 11, 2000): 8190–96. http://dx.doi.org/10.1074/jbc.m007235200.

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21

Swords, W. Edward, Miranda L. Moore, Luciana Godzicki, Gail Bukofzer, Michael J. Mitten, and Jessica VonCannon. "Sialylation of Lipooligosaccharides Promotes Biofilm Formation by Nontypeable Haemophilus influenzae." Infection and Immunity 72, no. 1 (January 2004): 106–13. http://dx.doi.org/10.1128/iai.72.1.106-113.2004.

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ABSTRACT Nontypeable Haemophilus influenzae (NTHi) is a major cause of opportunistic respiratory tract infections, including otitis media and bronchitis. The persistence of NTHi in vivo is thought to involve bacterial persistence in a biofilm community. Therefore, there is a need for further definition of bacterial factors contributing to biofilm formation by NTHi. Like other bacteria inhabiting host mucosal surfaces, NTHi has on its surface a diverse array of lipooligosaccharides (LOS) that influence host-bacterial interactions. In this study, we show that LOS containing sialic (N-acetyl-neuraminic) acid promotes biofilm formation by NTHi in vitro and bacterial persistence within the middle ear or lung in vivo. LOS from NTHi in biofilms was sialylated, as determined by comparison of electrophoretic mobilities and immunochemical reactivities before and after neuraminidase treatment. Biofilm formation was significantly reduced in media lacking sialic acid, and a siaB (CMP-sialic acid synthetase) mutant was deficient in biofilm formation in three different in vitro model systems. The persistence of an asialylated siaB mutant was attenuated in a gerbil middle ear infection model system, as well as in a rat pulmonary challenge model system. These data show that sialylated LOS glycoforms promote biofilm formation by NTHi and persistence in vivo.

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22

Matthews, Melissa M., John B. McArthur, Yanhong Li, Hai Yu, Xi Chen, and Andrew J. Fisher. "Catalytic Cycle of Neisseria meningitidis CMP-Sialic Acid Synthetase Illustrated by High-Resolution Protein Crystallography." Biochemistry 59, no. 34 (October 4, 2019): 3157–68. http://dx.doi.org/10.1021/acs.biochem.9b00517.

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23

STOUGHTON, Daniel M., Gerardo ZAPATA, Robert PICONE, and Willie F. VANN. "Identification of Arg-12 in the active site of Escherichia coli K1 CMP-sialic acid synthetase." Biochemical Journal 343, no. 2 (October 15, 1999): 397. http://dx.doi.org/10.1042/0264-6021:3430397.

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24

Kalpana. "BIOTRANSFORMATION USING RECOMBINANT CMP SIALIC ACID SYNTHETASE AND Î±-2, 6-SIALYLTRAN SFERASE: ENZYMATIC SYNTHESIS OF SIALOSIDES." American Journal of Biochemistry and Biotechnology 8, no. 4 (April 1, 2012): 288–303. http://dx.doi.org/10.3844/ajbbsp.2012.288.303.

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25

Fujita, Akiko, Chihiro Sato, and Ken Kitajima. "Identification of the nuclear export signals that regulate the intracellular localization of the mouse CMP-sialic acid synthetase." Biochemical and Biophysical Research Communications 355, no. 1 (March 2007): 174–80. http://dx.doi.org/10.1016/j.bbrc.2007.01.139.

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26

Knorst, Marion, and Wolf-Dieter Fessner. "CMP-Sialate Synthetase fromNeisseria meningitidis− Overexpression and Application to the Synthesis of Oligosaccharides Containing Modified Sialic Acids." Advanced Synthesis & Catalysis 343, no. 6-7 (August 2001): 698–710. http://dx.doi.org/10.1002/1615-4169(200108)343:6/7<698::aid-adsc698>3.0.co;2-j.

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27

Greiner, L. L., H. Watanabe, N. J. Phillips, J. Shao, A. Morgan, A. Zaleski, B. W. Gibson, and M. A. Apicella. "Nontypeable Haemophilus influenzae Strain 2019 Produces a Biofilm Containing N-Acetylneuraminic Acid That May Mimic Sialylated O-Linked Glycans." Infection and Immunity 72, no. 7 (July 2004): 4249–60. http://dx.doi.org/10.1128/iai.72.7.4249-4260.2004.

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ABSTRACT Previous studies suggested that nontypeable Haemophilus influenzae (NTHI) can form biofilms during human and chinchilla middle ear infections. Microscopic analysis of a 5-day biofilm of NTHI strain 2019 grown in a continuous-flow chamber revealed that the biofilm had a diffuse matrix interlaced with multiple water channels. Our studies showed that biofilm production was significantly decreased when a chemically defined medium lacking N-acetylneuraminic acid (sialic acid) was used. Based on these observations, we examined mutations in seven NTHI strain 2019 genes involved in carbohydrate and lipooligosaccharide biosynthesis. NTHI strain 2019 with mutations in the genes encoding CMP-N-acetylneuraminic acid synthetase (siaB), one of the three NTHI sialyltransferases (siaA), and the undecaprenyl-phosphate α-N-acetylglucosaminyltransferase homolog (wecA) produced significantly smaller amounts of biofilm. NTHI strain 2019 with mutations in genes encoding phosphoglucomutase (pgm), UDP-galactose-4-epimerase, and two other NTHI sialyltransferases (lic3A and lsgB) produced biofilms that were equivalent to or larger than the biofilms produced by the parent strain. The biofilm formed by the NTHI strain 2019pgm mutant was studied with Maackia amurensis fluorescein isothiocyanate (FITC)-conjugated and Sambucus nigra tetramethyl rhodamine isocyanate (TRITC)-conjugated lectins. S. nigra TRITC-conjugated lectin bound to this biofilm, while M. amurensis FITC-conjugated lectin did not. S. nigra TRITC-conjugated lectin binding was inhibited by incubation with α2,6-neuraminyllactose and by pretreatment of the biofilm with Vibrio cholerae neuraminidase. Matrix-assisted laser desorption ionization—time of flight mass spectometry analysis of lipooligosaccharides isolated from a biofilm, the planktonic phase, and plate-grown organisms showed that the levels of most sialylated glycoforms were two- to fourfold greater when the lipooligosaccharide was derived from planktonic or biofilm organisms. Our data indicate that NTHI strain 2019 produces a biofilm containing α2,6-linked sialic acid and that the sialic acid content of the lipooligosaccharides increases concomitant with the transition of organisms to a biofilm form.

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28

Nakata, D., A. K. Munster, R. Gerardy-Schahn, N. Aoki, T. Matsuda, and K. Kitajima. "Molecular cloning of a unique CMP-sialic acid synthetase that effectively utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid (Neu5Ac) as substrates." Glycobiology 11, no. 8 (August 1, 2001): 685–92. http://dx.doi.org/10.1093/glycob/11.8.685.

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29

Tiralongo, J., A. Fujita, C. Sato, K. Kitajima, F. Lehmann, M. Oschlies, R. Gerardy-Schahn, and A. K. Munster-Kuhnel. "The rainbow trout CMP-sialic acid synthetase utilises a nuclear localization signal different from that identified in the mouse enzyme." Glycobiology 17, no. 9 (April 18, 2007): 945–54. http://dx.doi.org/10.1093/glycob/cwm064.

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30

Spinola, Stanley M., Wei Li, Kate R. Fortney, Diane M. Janowicz, Beth Zwickl, Barry P. Katz, and Robert S. Munson. "Sialylation of Lipooligosaccharides Is Dispensable for the Virulence of Haemophilus ducreyi in Humans." Infection and Immunity 80, no. 2 (December 5, 2011): 679–87. http://dx.doi.org/10.1128/iai.05826-11.

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ABSTRACTSialylated glycoconjugates on the surfaces of mammalian cells play important roles in intercellular communication and self-recognition. The sialic acid preferentially expressed in human tissues isN-acetylneuraminic acid (Neu5Ac). In a process called molecular mimicry, many bacterial pathogens decorate their cell surface glycolipids with Neu5Ac. Incorporation of Neu5Ac into bacterial glycolipids promotes bacterial interactions with host cell receptors called Siglecs. These interactions affect bacterial adherence, resistance to serum killing and phagocytosis, and innate immune responses.Haemophilus ducreyi, the etiologic agent of chancroid, expresses lipooligosaccharides (LOS) that are highly sialylated. However, anH. ducreyisialyltransferase (lst) mutant, whose LOS contain reduced levels of Neu5Ac, is fully virulent in human volunteers. Recently, a second sialyltransferase gene (Hd0053) was discovered inH. ducreyi, raising the possibility thatHd0053compensated for the loss oflstduring human infection. CMP-Neu5Ac is the obligate nucleotide sugar donor for all bacterial sialyltransferases; LOS derived from anH. ducreyiCMP-Neu5Ac synthetase (neuA) mutant has no detectable Neu5Ac. Here, we compared anH. ducreyi neuAmutant to its wild-type parent in several models of pathogenesis. In human inoculation experiments, theneuAmutant formed papules and pustules at rates that were no different than those of its parent. When grown in media with and without Neu5Ac supplementation, theneuAmutant and its parent had similar phenotypes in bactericidal, macrophage uptake, and dendritic cell activation assays. Although we cannot preclude a contribution of LOS sialylation to ulcerative disease, these data strongly suggest that sialylation of LOS is dispensable forH. ducreyipathogenesis in humans.

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31

Ganguli, S., G. Zapata, T. Wallis, C. Reid, G. Boulnois, W. F. Vann, and I. S. Roberts. "Molecular cloning and analysis of genes for sialic acid synthesis in Neisseria meningitidis group B and purification of the meningococcal CMP-NeuNAc synthetase enzyme." Journal of Bacteriology 176, no. 15 (1994): 4583–89. http://dx.doi.org/10.1128/jb.176.15.4583-4589.1994.

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32

Niculovic, Kristina M., Linda Blume, Henri Wedekind, Elina Kats, Iris Albers, Stephanie Groos, Markus Abeln, et al. "Podocyte-Specific Sialylation-Deficient Mice Serve as a Model for Human FSGS." Journal of the American Society of Nephrology 30, no. 6 (April 30, 2019): 1021–35. http://dx.doi.org/10.1681/asn.2018090951.

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BackgroundThe etiology of steroid-resistant nephrotic syndrome, which manifests as FSGS, is not completely understood. Aberrant glycosylation is an often underestimated factor for pathologic processes, and structural changes in the glomerular endothelial glycocalyx have been correlated with models of nephrotic syndrome. Glycans are frequently capped by sialic acid (Sia), and sialylation’s crucial role for kidney function is well known. Human podocytes are highly sialylated; however, sialylation’s role in podocyte homeostasis remains unclear.MethodsWe generated a podocyte-specific sialylation-deficient mouse model (PCmas−/−) by targeting CMP-Sia synthetase, and used histologic and ultrastructural analysis to decipher the phenotype. We applied CRISPR/Cas9 technology to generate immortalized sialylation-deficient podocytes (asialo-podocytes) for functional studies.ResultsProgressive loss of sialylation in PCmas−/− mice resulted in onset of proteinuria around postnatal day 28, accompanied by foot process effacement and loss of slit diaphragms. Podocyte injury led to severe glomerular defects, including expanded capillary lumen, mesangial hypercellularity, synechiae formation, and podocyte loss. In vivo, loss of sialylation resulted in mislocalization of slit diaphragm components, whereas podocalyxin localization was preserved. In vitro, asialo-podocytes were viable, able to proliferate and differentiate, but showed impaired adhesion to collagen IV.ConclusionsLoss of cell-surface sialylation in mice resulted in disturbance of podocyte homeostasis and FSGS development. Impaired podocyte adhesion to the glomerular basement membrane most likely contributed to disease development. Our data support the notion that loss of sialylation might be part of the complex process causing FSGS. Sialylation, such as through a Sia supplementation therapy, might provide a new therapeutic strategy to cure or delay FSGS and potentially other glomerulopathies.

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Knorst, Marion, and Wolf-Dieter Fessner. "ChemInform Abstract: Enzymes in Organic Synthesis. Part 18. CMP-Sialate Synthetase from Neisseria meningitidis - Overexpression and Application to the Synthesis of Oligosaccharides Containing Modified Sialic Acids." ChemInform 32, no. 49 (May 23, 2010): no. http://dx.doi.org/10.1002/chin.200149247.

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Mizanur, Rahman M., and Nicola L. Pohl. "Bacterial CMP-sialic acid synthetases: production, properties, and applications." Applied Microbiology and Biotechnology 80, no. 5 (October 2008). http://dx.doi.org/10.1007/s00253-008-1643-7.

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Di, Wu, Akiko Fujita, Kayo Hamaguchi, Philippe Delannoy, Chihiro Sato, and Ken Kitajima. "Diverse subcellular localizations of the insect CMP-sialic acid synthetases." Glycobiology, December 16, 2016. http://dx.doi.org/10.1093/glycob/cww128.

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Ng, Preston S. K., Christopher J. Day, John M. Atack, Lauren E. Hartley-Tassell, Linda E. Winter, Tal Marshanski, Vered Padler-Karavani, et al. "NontypeableHaemophilus influenzaeHas Evolved Preferential Use ofN-Acetylneuraminic Acid as a Host Adaptation." mBio 10, no. 3 (May 7, 2019). http://dx.doi.org/10.1128/mbio.00422-19.

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ABSTRACTNontypeableHaemophilus inﬂuenzae(NTHi) is a Gram-negative bacterial pathogen that is adapted exclusively to human hosts. NTHi utilizes sialic acid from the host as a carbon source and as a terminal sugar on the outer membrane glycolipid lipooligosaccharide (LOS). Sialic acid expressed on LOS is critical in NTHi biofilm formation and immune evasion. There are two major forms of sialic acids in most mammals,N-acetylneuraminic acid (Neu5Ac) andN-glycolylneuraminic acid (Neu5Gc), the latter of which is derived from Neu5Ac. Humans lack the enzyme to convert Neu5Ac to Neu5Gc and do not express Neu5Gc in normal tissues; instead, Neu5Gc is recognized as a foreign antigen. A recent study showed that dietary Neu5Gc can be acquired by NTHi colonizing humans and then presented on LOS, which acts as an antigen for the initial induction of anti-Neu5Gc antibodies. Here we examined Neu5Gc uptake and presentation on NTHi LOS. We show that, although Neu5Gc and Neu5Ac are utilized equally well as sole carbon sources, Neu5Gc is not incorporated efficiently into LOS. When equal amounts of Neu5Gc and Neu5Ac are provided in culture media, there is ∼4-fold more Neu5Ac incorporated into LOS, suggesting a bias in a step of the LOS biosynthetic pathway. CMP-Neu5Ac synthetase (SiaB) was shown to have ∼4,000-fold-higher catalytic efficiency for Neu5Ac than for Neu5Gc. These data suggest that NTHi has adapted preferential utilization of Neu5Ac, thus avoiding presentation of the nonhuman Neu5Gc in the bacterial cell surface. The selective pressure for this adaptation may represent the human antibody response to the Neu5Gc xenoantigen.IMPORTANCEHost-adapted bacterial pathogens such as NTHi cannot survive out of their host environment and have evolved host-specific mechanisms to obtain nutrients and evade the immune response. Relatively few of these host adaptations have been characterized at the molecular level. NTHi utilizes sialic acid as a nutrient and also incorporates this sugar into LOS, which is important in biofilm formation and immune evasion. In the present study, we showed that NTHi has evolved to preferentially utilize the Neu5Ac form of sialic acid. This adaptation is due to the substrate preference of the enzyme CMP-Neu5Ac synthetase, which synthesizes the activated form of Neu5Ac for macromolecule biosynthesis. This adaptation allows NTHi to evade killing by a human antibody response against the nonhuman sialic acid Neu5Gc.

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Wu, Di, Hiromu Arakawa, Akiko Fujita, Hisashi Hashimoto, Masahiko Hibi, Kiyoshi Naruse, Yasuhiro Kamei, Chihiro Sato, and Ken Kitajima. "A point-mutation in the C-domain of CMP-sialic acid synthetase leads to lethality of medaka due to protein insolubility." Scientific Reports 11, no. 1 (December 2021). http://dx.doi.org/10.1038/s41598-021-01715-3.

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AbstractVertebrate CMP-sialic acid synthetase (CSS), which catalyzes the synthesis of CMP-sialic acid (CMP-Sia), consists of a 28 kDa-N-domain and a 20 kDa-C-domain. The N-domain is known to be a catalytic domain; however, the significance of the C-domain still remains unknown. To elucidate the function of the C-domain at the organism level, we screened the medaka TILLING library and obtained medaka with non-synonymous mutations (t911a), or single amino acid substitutions of CSS, L304Q, in the C-domain. Prominently, most L304Q medaka was lethal within 19 days post-fertilization (dpf). L304Q young fry displayed free Sia accumulation, and impairment of sialylation, up to 8 dpf. At 8 dpf, a marked abnormality in ventricular contraction and skeletal myogenesis was observed. To gain insight into the mechanism of L304Q-induced abnormalities, L304Q was biochemically characterized. Although bacterially expressed soluble L304Q and WT showed the similar Vmax/Km values, very few soluble L304Q was detected when expressed in CHO cells in sharp contrast to the WT. Additionally, the thermostability of various mutations of L304 greatly decreased, except for WT and L304I. These results suggest that L304 is important for the stability of CSS, and that an appropriate level of expression of soluble CSS is significant for animal survival.

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Wu, Di, Pierre-André Gilormini, Sakura Toda, Christophe Biot, Cédric Lion, Yann Guérardel, Chihiro Sato, and Ken Kitajima. "A novel C-domain-dependent inhibition of the rainbow trout CMP-sialic acid synthetase activity by CMP-deaminoneuraminic acid." Biochemical and Biophysical Research Communications, May 2022. http://dx.doi.org/10.1016/j.bbrc.2022.05.031.

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Schelch, Sabine, Romana Koszagova, Jürgen Kuballa, and Bernd Nidetzky. "Immobilization of CMP‐Sialic Acid Synthetase and α2,3‐Sialyltransferase for Cascade Synthesis of 3′‐Sialyl β‐D‐Galactoside with Enzyme Reuse." ChemCatChem, March 30, 2022. http://dx.doi.org/10.1002/cctc.202101860.

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