title: Histochemical fluorescent staining of Sendai virus-infected cells with a novel sialidase substrate.
abstract: Sialidases, enzymes that remove terminal sialic acid residues, are pivotal in various biological processes such as malignancy and infection with pathogens. For histochemical staining of sialidase activity, we have developed a new synthetic sialidase substrate, sialic acid-conjugated fluorescent benzothiazolylphenol derivative (BTP3-Neu5Ac), for rapid, sensitive, and specific fluorescent staining of sialidase activity. Here, we showed the usefulness of BTP3-Neu5Ac for histochemical fluorescent staining of cells infected with Sendai virus (SV), which possesses sialidase activity. BTP3-Neu5Ac also visualised SV-infected regions of lung sections from SV-infected mice. We succeeded in histochemical fluorescent staining of SV both in vitro and in vivo. SV has been utilised in many virological and biotechnological studies such as developments of an oncolytic virus, a gene therapy vector, and a vaccine candidate. BTP3-Neu5Ac should contribute to rapid progress of such studies and researches on viral sialidase.
authors.affiliation: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka-shi, Shizuoka 4228526, Japan.
authors.forename: Maiko
authors.initials: M
authors.lastname: Takano
authors.affiliation: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka-shi, Shizuoka 4228526, Japan.
authors.forename: Tadanobu
authors.initials: T
authors.lastname: Takahashi
authors.affiliation: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka-shi, Shizuoka 4228526, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Agarikuchi
authors.affiliation: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka-shi, Shizuoka 4228526, Japan.
authors.forename: Yuuki
authors.initials: Y
authors.lastname: Kurebayashi
authors.affiliation: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka-shi, Shizuoka 4228526, Japan.
authors.forename: Akira
authors.initials: A
authors.lastname: Minami
authors.affiliation: Department of Organic Chemistry, School of Pharmaceutical Sciences, Hiroshima International University, Kure-shi, Hiroshima 7370112, Japan.
authors.forename: Tadamune
authors.initials: T
authors.lastname: Otsubo
authors.affiliation: Department of Organic Chemistry, School of Pharmaceutical Sciences, Hiroshima International University, Kure-shi, Hiroshima 7370112, Japan.
authors.forename: Kiyoshi
authors.initials: K
authors.lastname: Ikeda
authors.affiliation: Department of Functional Anatomy, School of Nursing, University of Shizuoka, Shizuoka-shi, Shizuoka 4228526, Japan.
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Kanazawa
authors.affiliation: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka-shi, Shizuoka 4228526, Japan. Electronic address: suzukit@u-shizuoka-ken.ac.jp.
authors.forename: Takashi
authors.initials: T
authors.lastname: Suzuki
mesh_terms: D052160:Benzothiazoles / Q000737:chemistry / Q000378:metabolism; D005456:Fluorescent Dyes / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D019158:N-Acetylneuraminic Acid / Q000737:chemistry / Q000378:metabolism; D009439:Neuraminidase / Q000737:chemistry* / Q000378:metabolism; D010253:Respirovirus Infections / Q000175:diagnosis / Q000821:virology*; D029082:Sendai virus / Q000737:chemistry / Q000201:enzymology*; D013194:Staining and Labeling / Q000295:instrumentation / Q000379:methods*; D013379:Substrate Specificity; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D052160:Benzothiazoles; D005456:Fluorescent Dyes; D014764:Viral Proteins; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid
keywords: Easy protocol; Fluorescent staining; Hemagglutinin-neuraminidase; Histochemical staining; Infection detection; Rapid protocol; Sendai virus; Sensitive detection; Sialidase activity; Synthetic substrate