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Journal articles on the topic 'ChiTn antibody'

Author: Grafiati

Published: 5 June 2025

Last updated: 2 August 2025

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1

Ryan, G. B., W. T. Jones, R. E. Mitchell, and V. Mett. "Polyclonal Antibody Production Against Chito-Oligosaccharides." Food and Agricultural Immunology 13, no. 2 (2001): 127–30. http://dx.doi.org/10.1080/09540100120055600.

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2

Tokura, Seiichi, Osatoshi Hasegawa, Shin-Ichiro Nishimura, Norio Nishi, and Takehiko Takatori. "Induction of methamphetamine-specific antibody using biodegradable carboxymethyl-chitin." Analytical Biochemistry 161, no. 1 (1987): 117–22. http://dx.doi.org/10.1016/0003-2697(87)90660-9.

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3

Grabińska, Kariona A., Paula Magnelli, and Phillips W. Robbins. "Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III Activity and Chitin Chain Length." Eukaryotic Cell 6, no. 2 (2006): 328–36. http://dx.doi.org/10.1128/ec.00203-06.

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ABSTRACT Chs4p (Cal2/Csd4/Skt5) was identified as a protein factor physically interacting with Chs3p, the catalytic subunit of chitin synthase III (CSIII), and is indispensable for its enzymatic activity in vivo. Chs4p contains a putative farnesyl attachment site at the C-terminal end (CVIM motif) conserved in Chs4p of Saccharomyces cerevisiae and other fungi. Several previous reports questioned the role of Chs4p prenylation in chitin biosynthesis. In this study we reinvestigated the function of Chs4p prenylation. We provide evidence that Chs4p is farnesylated by showing that purified Chs4p is

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4

Sendid, B., N. Dotan, S. Nseir, et al. "Antibodies against Glucan, Chitin, and Saccharomyces cerevisiae Mannan as New Biomarkers of Candida albicans Infection That Complement Tests Based on C. albicans Mannan." Clinical and Vaccine Immunology 15, no. 12 (2008): 1868–77. http://dx.doi.org/10.1128/cvi.00200-08.

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ABSTRACT Antibodies against Saccharomyces cerevisiae mannan (ASCA) and antibodies against synthetic disaccharide fragments of glucans (ALCA) and chitin (ACCA) are biomarkers of Crohn's disease (CD). We previously showed that Candida albicans infection generates ASCA. Here, we explored ALCA and ACCA as possible biomarkers of invasive C. albicans infection (ICI). ASCA, ALCA, ACCA, and Candida mannan antigen and antibody detection tests were performed on 69 sera obtained sequentially from 18 patients with ICIs proven by blood culture, 59 sera from CD patients, 47 sera from hospitalized subjects c

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5

Fonseca, Fernanda L., Leonardo Nimrichter, Radames J. B. Cordero, et al. "Role for Chitin and Chitooligomers in the Capsular Architecture of Cryptococcus neoformans." Eukaryotic Cell 8, no. 10 (2009): 1543–53. http://dx.doi.org/10.1128/ec.00142-09.

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ABSTRACT Molecules composed of β-1,4-linked N-acetylglucosamine (GlcNAc) and deacetylated glucosamine units play key roles as surface constituents of the human pathogenic fungus Cryptococcus neoformans. GlcNAc is the monomeric unit of chitin and chitooligomers, which participate in the connection of capsular polysaccharides to the cryptococcal cell wall. In the present study, we evaluated the role of GlcNAc-containing structures in the assembly of the cryptococcal capsule. The in vivo expression of chitooligomers in C. neoformans varied depending on the infected tissue, as inferred from the di

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6

Ju, Ruibao, Yanjing Lu, Zhiwen Jiang, et al. "A Thermosensitive and Degradable Chitin-Based Hydrogel as a Brucellosis Vaccine Adjuvant." Polymers 16, no. 19 (2024): 2815. http://dx.doi.org/10.3390/polym16192815.

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Brucellosis is a zoonotic infectious disease that has long endangered the development of animal husbandry and human health. Currently, vaccination stands as the most efficacious method for preventing and managing brucellosis. Alum, as the most commonly used adjuvant for the brucellosis vaccine, has obvious disadvantages, such as the formation of granulomas and its non-degradability. Therefore, the aims of this study were to prepare an absorbable, injectable, and biocompatible hydroxypropyl chitin (HPCT) thermosensitive hydrogel and to evaluate its immunization efficacy as an adjuvant for Bruce

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7

Stefanov, Emily, Nicolas Kin, Brian Dizon, and John Kearney. "Antibodies generated against conserved antigens suppress allergic airway disease (125.13)." Journal of Immunology 188, no. 1_Supplement (2012): 125.13. http://dx.doi.org/10.4049/jimmunol.188.supp.125.13.

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Abstract There has been a sharp rise in allergic asthma and asthma-related deaths in the developed world. The hygiene hypothesis proposes that excessively sanitary conditions early in life result in autoimmune and allergic phenomena because of a failure of the immune system to receive proper microbial stimulation during development. Chitin, a biopolymer of N-acetyl glucosamine (GlcNAc), is produced by many allergen-bearing organisms including: fungi, the exoskeleton of insects, crabs, shrimp and parasitic nematodes. We demonstrate that antibodies generated against chitin and other conserved ba

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8

Aguilar-Díaz, Hugo, Juan Pedro Laclette, and Julio César Carrero. "Silencing ofEntamoeba histolyticaGlucosamine 6-Phosphate Isomerase by RNA Interference Inhibits the Formation of Cyst-Like Structures." BioMed Research International 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/758341.

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Encystment is an essential process in the biological cycle of the human parasiteEntamoeba histolytica. In the present study, we evaluated the participation ofE. histolyticaGln6Pi in the formation of amoeba cyst-like structures by RNA interference assay. Amoeba trophozoites transfected with two Gln6Pi siRNAs reduced the expression of the enzyme in 85%, which was confirmed by western blot using an anti-Gln6Pi antibody. TheE. histolyticaGln6Pi knockdown with the mix of both siRNAs resulted in the loss of its capacity to form cyst-like structures (CLSs) and develop a chitin wall under hydrogen per

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9

Greppi, Chloe. "Cryosectioning and Immunohistochemistry of Peripheral Tissues of Mosquitoes." Cold Spring Harbor Protocols 2023, no. 1 (2022): pdb.prot107914. http://dx.doi.org/10.1101/pdb.prot107914.

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Immunohistochemistry analysis of mosquitoes is complicated by the outer cuticle that prevents reagents from penetrating peripheral tissues. This protocol incorporates a cryosectioning method that provides a higher resolution of the internal architecture of mosquito peripheral sensory tissues and enables the visualization of protein expression. This eliminates the need for enzymatic steps to digest the outer cuticle that encases these tissues. This protocol can also be adapted for other tissues, such as the brain and the legs, as chitin exoskeleton thickness does not affect antibody penetration

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10

DAVIES, D. R., and S. CHACKO. "ChemInform Abstract: Antibody Structure." ChemInform 24, no. 49 (2010): no. http://dx.doi.org/10.1002/chin.199349321.

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11

HILVERT, D. "ChemInform Abstract: Antibody Catalysis." ChemInform 23, no. 42 (2010): no. http://dx.doi.org/10.1002/chin.199242272.

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12

LI, T., R. A. LERNER, and K. D. JANDA. "ChemInform Abstract: Antibody-Catalyzed Cationic Reactions: Rerouting of Chemical Transformations via Antibody Catalysis." ChemInform 28, no. 27 (2010): no. http://dx.doi.org/10.1002/chin.199727296.

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13

Seiichi, Tokura, Miura Yoshiaki, Johmen Masayoshi, Nishi Norio, and Nishimura Shin-Ichiro. "Induction of drug specific antibody and the controlled release of drug by 6-O-carboxymethyl-chitin." Journal of Controlled Release 28, no. 1-3 (1994): 235–41. http://dx.doi.org/10.1016/0168-3659(94)90170-8.

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14

Li, Hao-Kang, Cheng-Wei Lai, Chien-Yu Lin, et al. "Abstract 1785: Development of dual-payload anti-GPC3 antibody-drug conjugate by dual-payload antibody conjugation (AD2C) platform for hepatocellular carcinoma treatment." Cancer Research 85, no. 8_Supplement_1 (2025): 1785. https://doi.org/10.1158/1538-7445.am2025-1785.

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Abstract Glypican-3 (GPC3) has been reported as a promising target for the treatment of hepatocellular carcinoma (HCC). Although current therapies are available, tumor heterogeneity and the development of drug resistance continue to pose significant challenges to effective treatment. Therefore, combination therapy has emerged as a promising strategy to address these challenges. Acepodia successfully established a Dual-Payload Antibody Conjugation (AD2C) platform utilizing our proprietary bioorthogonal chemistry, which allows conjugating two (or multiple) different payloads to the antibody with

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15

Minkova, Olga A., Еlena I. Yarygina, and Vera M. Rakova. "A study of the effect of chitosan in the vaccine on the immune response against Newcastle disease in broiler chickens." Veterinariya, Zootekhniya i Biotekhnologiya 4/2, no. 136 (2025): 33–42. https://doi.org/10.36871/vet.zoo.bio.202504203.

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Chitosan is a natural polymer that is produced from chitin of crustaceans by partial deacetylation of N-acetyl-D-glucosamine, safe, biocompatible, and has sorption properties [5]. Live vaccines against Newcastle bird disease, which are actively used in poultry farming, are reactogenic and have a relatively short protection period. Intranasal administration of chitosan together with the vaccine antigen can increase the immunogenicity of the vaccine, while reducing its reactogenic properties. The immunomodulatory activity of chitosan in combination with a vaccine against Newcastle disease was st

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16

Taylor, Matthew J., Timothy Z. Hoffman, Jari T. Yli-Kauhaluoma, Richard A. Lerner, and Kim D. Janda. "ChemInform Abstract: A Light-Activated Antibody Catalyst." ChemInform 30, no. 17 (2010): no. http://dx.doi.org/10.1002/chin.199917044.

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17

ZHOU, Z. S., N. JIANG, and D. HILVERT. "ChemInform Abstract: An Antibody-Catalyzed Selenoxide Elimination." ChemInform 28, no. 32 (2010): no. http://dx.doi.org/10.1002/chin.199732075.

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18

ULRICH, H. D., E. M. G. DRIGGERS, and P. G. SCHULTZ. "ChemInform Abstract: Antibody Catalysis of Pericyclic Reactions." ChemInform 27, no. 35 (2010): no. http://dx.doi.org/10.1002/chin.199635311.

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19

YU, J., L. C. HSIEH, L. KOCHERSPERGER, et al. "ChemInform Abstract: Progress Toward an Antibody Glycosidase." ChemInform 25, no. 22 (2010): no. http://dx.doi.org/10.1002/chin.199422050.

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20

Marcos, Caroline Maria, Haroldo Cesar de Oliveira, Patrícia Akemi Assato, Rafael Fernando Castelli, Ana Marisa Fusco-Almeida, and Maria José Soares Mendes-Giannini. "Drk1, a Dimorphism Histidine Kinase, Contributes to Morphology, Virulence, and Stress Adaptation in Paracoccidioides brasiliensis." Journal of Fungi 7, no. 10 (2021): 852. http://dx.doi.org/10.3390/jof7100852.

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P. brasiliensis is a thermally dimorphic fungus belonging to Paracoccidioides complex, causative of a systemic, endemic mycosis limited to Latin American countries. Signal transduction pathways related to important aspects as surviving, proliferation according to the biological niches are linked to the fungal pathogenicity in many species, but its elucidation in P. brasiliensis remains poorly explored. As Drk1, a hybrid histidine kinase, plays regulators functions in other dimorphic fungi species, mainly in dimorphism and virulence, here we investigated its importance in P. brasilensis. We, th

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21

Pendland, J. C., and D. G. Boucias. "Ultrastructural localization of carbohydrate in cell walls of the entomogenous hyphomycete Nomuraea rileyi." Canadian Journal of Microbiology 38, no. 5 (1992): 377–86. http://dx.doi.org/10.1139/m92-064.

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Several probes were used in this ultrastructural study to localize polysaccharides in cell walls on conidial germ tubes, hyphal bodies, and mycelia of the entomogenous hyphomycete Nomuraea rileyi. With the exception of galactose, labelling patterns did not vary from one morphological stage to another. Galactose, which was localized by using a monoclonal antibody to a galactose-specific lectin purified from insect larval hemolymph, was absent from cell walls of hyphal bodies and conidia but was present on germ-tube and mycelial surfaces. Chitin (N-acetylglucosamine), labelled with a wheat-germ

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22

SCHULTZ, P. G., and R. A. LERNER. "ChemInform Abstract: Antibody Catalysis of Difficult Chemical Transformations." ChemInform 24, no. 49 (2010): no. http://dx.doi.org/10.1002/chin.199349319.

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23

Hasserodt, Jens. "ChemInform Abstract: Organic Synthesis Supported by Antibody Catalysis." ChemInform 31, no. 9 (2010): no. http://dx.doi.org/10.1002/chin.200009257.

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24

IKEDA, S., M. I. WEINHOUSE, K. D. JANDA, R. A. LERNER, and S. J. DANISHEFSKY. "ChemInform Abstract: Asymmetric Induction via a Catalytic Antibody." ChemInform 23, no. 1 (2010): no. http://dx.doi.org/10.1002/chin.199201074.

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25

KEINAN, E., S. C. SINHA, A. SINHA-BAGCHI, et al. "ChemInform Abstract: Towards Antibody-Mediated Metallo-Porphyrin Chemistry." ChemInform 22, no. 7 (2010): no. http://dx.doi.org/10.1002/chin.199107336.

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26

REYMOND, J. L., G. K. JAHANGIRI, C. STOUDT, and R. A. LERNER. "ChemInform Abstract: Antibody-Catalyzed Hydrolysis of Enol Ethers." ChemInform 24, no. 39 (2010): no. http://dx.doi.org/10.1002/chin.199339085.

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27

REYMOND, J. L., K. D. JANDA, and R. A. LERNER. "ChemInform Abstract: Antibody Catalysis of Glycosidic Bond Hydrolysis." ChemInform 23, no. 10 (2010): no. http://dx.doi.org/10.1002/chin.199210071.

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28

SCANLAN, T. S., J. R. PRUDENT, and P. G. SCHULTZ. "ChemInform Abstract: Antibody-Catalyzed Hydrolysis of Phosphate Monoesters." ChemInform 23, no. 12 (2010): no. http://dx.doi.org/10.1002/chin.199212102.

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29

Lampe, Anna T., Eric J. Farris, Matthew D. Ballweg, Angela K. Pannier, and Deborah M. Brown. "Non-complexed chitosan acts as an adjuvant in an influenza A virus protein vaccine." Journal of Immunology 202, no. 1_Supplement (2019): 139.14. http://dx.doi.org/10.4049/jimmunol.202.supp.139.14.

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Abstract During the 2017–18 season influenza A virus (IAV) induced significant morbidity and mortality with the most recent vaccine estimated to be 36% effective in preventing illness. However, IAV vaccines may be improved through the use of adjuvants that enhance or direct specific immune responses. The biomaterial chitosan (CS), a partially deacetylated derivative of chitin, has been used in nucleic acid vaccine strategies for its ability to complex with DNA to form nanoparticles. However, we and others have found that non-complexed CS induces cell death and proinflammatory cytokine response

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30

Cordova, Armando, and Kim D. Janda. "ChemInform Abstract: Synthesis and Catalytic Antibody Functionalization of Dendrimers." ChemInform 32, no. 51 (2010): no. http://dx.doi.org/10.1002/chin.200151083.

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31

JANDA, K. D., C. G. SHEVLIN, and R. A. LERNER. "ChemInform Abstract: Antibody Catalysis of a Disfavored Chemical Transformation." ChemInform 24, no. 16 (2010): no. http://dx.doi.org/10.1002/chin.199316068.

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32

List, Benjamin, Richard A. Lerner, and Carlos F. Barbas III. "ChemInform Abstract: Enantioselective Aldol Cyclodehydrations Catalyzed by Antibody 38C2." ChemInform 30, no. 42 (2010): no. http://dx.doi.org/10.1002/chin.199942090.

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33

GIBBS, R. A., S. TAYLOR, and S. J. BENKOVIC. "ChemInform Abstract: Antibody-Catalyzed Rearrangement of the Peptide Bond." ChemInform 24, no. 6 (2010): no. http://dx.doi.org/10.1002/chin.199306276.

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34

PARKER, D. "ChemInform Abstract: Tumour Targeting with Radiolabelled Macrocycle-Antibody Conjugates." ChemInform 22, no. 5 (2010): no. http://dx.doi.org/10.1002/chin.199105359.

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35

WADE, W. S., J. A. ASHLEY, G. K. JAHANGIRI, G. MCELHANEY, K. D. JANDA, and R. A. LERNER. "ChemInform Abstract: A Highly Specific Metal-Activated Catalytic Antibody." ChemInform 24, no. 41 (2010): no. http://dx.doi.org/10.1002/chin.199341064.

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36

KITAZUME, T., J. T. LIN, T. YAMAMOTO, and T. YAMAZAKI. "ChemInform Abstract: Antibody-Catalyzed Double Stereoselection in Fluorinated Materials." ChemInform 23, no. 8 (2010): no. http://dx.doi.org/10.1002/chin.199208058.

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37

Maggiotti, Virginie, Marina Resmini, and Veronique Gouverneur. "ChemInform Abstract: Unprecedented Regiocontrol Using an Aldolase I Antibody." ChemInform 33, no. 29 (2010): no. http://dx.doi.org/10.1002/chin.200229048.

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38

BRAISTED, A. C., and P. G. SCHULTZ. "ChemInform Abstract: An Antibody-Catalyzed Bimolecular Diels-Alder Reaction." ChemInform 22, no. 3 (2010): no. http://dx.doi.org/10.1002/chin.199103067.

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39

Tremblay, Martin R., Tobin J. Dickerson, and Kim D. Janda. "ChemInform Abstract: Advances in Antibody Catalysis of Cycloaddition Reactions." ChemInform 32, no. 49 (2010): no. http://dx.doi.org/10.1002/chin.200149280.

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40

REYMOND, J. L., K. D. JANDA, and R. A. LERNER. "ChemInform Abstract: Highly Enantioselective Protonation Catalyzed by an Antibody." ChemInform 23, no. 27 (2010): no. http://dx.doi.org/10.1002/chin.199227073.

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41

Mitchell, Alison J., Katie A. Hutchison, Naomi A. Pain, James A. Callow, and Jonathan R. Green. "A monoclonal antibody that recognizes a carbohydrate epitope on N-linked glycoproteins restricted to a subset of chitin-rich fungi." Mycological Research 101, no. 1 (1997): 73–79. http://dx.doi.org/10.1017/s095375629600216x.

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42

KIKUCHI, K., and D. HILVERT. "ChemInform Abstract: Antibody Catalysis via Strategic Use of Haptenic Charge." ChemInform 27, no. 35 (2010): no. http://dx.doi.org/10.1002/chin.199635312.

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43

NORMAN, T. J., D. PARKER, L. ROYLE, A. HARRISON, P. ANTONIW, and D. J. KING. "ChemInform Abstract: Improved Tumor Targeting with Recombinant Antibody-Macrocycle Conjugates." ChemInform 27, no. 5 (2010): no. http://dx.doi.org/10.1002/chin.199605257.

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44

Constantinou, Antony, Chen Chen, and Mahendra P. Deonarain. "ChemInform Abstract: Polysialic Acid and Polysialylation to Modulate Antibody Pharmacokinetics." ChemInform 44, no. 26 (2013): no. http://dx.doi.org/10.1002/chin.201326207.

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45

Ono, Mitsunori, and Yumiko Wada. "ChemInform Abstract: Study on Substrate Specificity of Hydrolytic Catalytic Antibody." ChemInform 31, no. 22 (2010): no. http://dx.doi.org/10.1002/chin.200022289.

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46

Shulman, Avidor, Danielle Sitry, Hagit Shulman, and Ehud Keinan. "ChemInform Abstract: Highly Efficient Antibody-Catalyzed Deuteration of Carbonyl Compounds." ChemInform 33, no. 19 (2010): no. http://dx.doi.org/10.1002/chin.200219066.

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47

Ostler, Elizabeth L., Marina Resmini, Guillaume Boucher, Nickolas Romanov, Keith Brocklehurst та Gerard Gallacher. "ChemInform Abstract: Polyclonal Antibody-Catalyzed Hydrolysis of a β-Lactam." ChemInform 33, № 19 (2010): no. http://dx.doi.org/10.1002/chin.200219243.

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48

REYMOND, J. L., J. L. REBER, and R. A. LERNER. "ChemInform Abstract: Enantioselective, Multigram-Scale Synthesis with a Catalytic Antibody." ChemInform 25, no. 24 (2010): no. http://dx.doi.org/10.1002/chin.199424059.

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49

Brown, Deborah M., Anna T. Lampe, Eric Farris, James A. Williams, and Angela K. Pannier. "Chitosan nanoparticle delivery of Influenza A Virus DNA vaccine enhances antibody class switching and abrogates weight loss post IAV challenge." Journal of Immunology 198, no. 1_Supplement (2017): 147.3. http://dx.doi.org/10.4049/jimmunol.198.supp.147.3.

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Abstract DNA vaccination presents a promising new approach for Influenza A Virus (IAV) vaccines, as they can be generated quickly in response to the viral antigenic shift and drift characteristic of IAV pandemic outbreaks. A DNA vaccination approach for IAV was examined using a plasmid encoding PR8 H1N1 hemagglutinin (HA) protein as a potential IAV vaccine. In addition to the HA antigen sequence the plasmid also encoded a sequence that when transcribed, activates the pattern recognition receptor RIG-I, improving innate immune activation. To increase the potential of this IAV DNA vaccine, our s

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50

Altay Benetti, Ayça, Eugene Yang Zhi Tan, Zi Wei Chang, et al. "Design and Characterization of a New Formulation for the Delivery of COVID-19-mRNA Vaccine to the Nasal Mucosa." Vaccines 12, no. 4 (2024): 409. http://dx.doi.org/10.3390/vaccines12040409.

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Chitosan, a natural polysaccharide derived from chitin, possesses biocompatibility, biodegradability, and mucoadhesive characteristics, making it an attractive material for the delivery of mRNA payloads to the nasal mucosa and promoting their uptake by target cells such as epithelial and immune cells (e.g., dendritic cells and macrophages). In this project, we aimed at developing novel lipid-based nanoformulations for mRNA delivery to counteract the pandemic caused by SARS-CoV-2 virus. The formulations achieved a mRNA encapsulation efficiency of ~80.2% with chitosan-lipid nanoparticles, as mea

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