Regular Article
Silkworm Hemolymph Inhibits Baculovirus-Induced Insect Cell Apoptosis

https://doi.org/10.1006/bbrc.2000.2592Get rights and content

Abstract

The effect of silkworm hemolymph on baculovirus-induced insect cell apoptosis was investigated. The addition of silkworm hemolymph into the culture medium either before or during the baculovirus infection increased the host cell longevity; however, its addition after the infection was less effective. This can be explained by the higher transfer rate of silkworm hemolymph which is caused by endocytosis during the virus internalization step. The delayed cell death due to silkworm hemolymph was not caused by an inhibition of the virus attachment and internalization steps. The apoptosis was analyzed using DNA fragmentation and TUNEL assays, and the resulting data confirm that silkworm hemolymph inhibits baculovirus-induced insect cell apoptosis.

References (27)

  • S. Henderson et al.

    Cell

    (1991)
  • R.R. Granados et al.
  • R.J. Clem et al.

    Science

    (1991)
  • S.G. Kamito et al.

    J. Virol.

    (1993)
  • D. Hockenbery et al.

    Nature

    (1990)
  • E. Yonish-Rauach et al.

    Nature

    (1991)
  • N.E. Crook et al.

    J. Virol.

    (1993)
  • M.J. Birnbaum et al.

    J. Virol.

    (1994)
  • P. Liston et al.

    Nature

    (1996)
  • C.S. Duckett et al.

    EMBO J.

    (1996)
  • S.S. Wyatt

    J. Gen. Physiol.

    (1956)
  • G.R. Wyatt et al.

    J. Gen. Physiol.

    (1956)
  • T.D.C. Grace

    Nature

    (1962)
  • Cited by (60)

    • Protein-based direct reprogramming of fibroblasts to neuronal cells using 30Kc19 protein and transcription factor Ascl1

      2020, International Journal of Biochemistry and Cell Biology
      Citation Excerpt :

      30Kc19 protein is derived from hemolymph of silkworm, Bombyx mori, and it is a member of the 30K protein family (Kim et al., 2003). Previously, we have observed various effects of silkworm hemolymph (Ha et al., 1996; Ha and Park, 1997; Rhee et al., 1999; Rhee and Park, 2000; Choi et al., 2002; Rhee et al., 2002; Choi et al., 2005) and 30K protein (Kim and Park, 2003; Kim et al., 2004; Choi et al., 2006; Wang et al., 2011; Park et al., 2015) by gene expression or addition of recombinant proteins. Since then, cell-penetrating and enzyme-stabilizing effect of 30Kc19 protein have been demonstrated (Park et al., 2012a, b).

    • Enhanced single-cell viability using 30Kc6 for efficient expansion of human induced pluripotent stem cells

      2019, Process Biochemistry
      Citation Excerpt :

      Similarly, we recently used the 30 Kc6 protein to increase single cell viability. The 30 Kc6 protein derived from Bombyx mori exhibits anti-apoptotic properties against insect cells [17–21] and mammalian cells [22–24]. The mechanism of apoptosis inhibition by 30 Kc6 was shown to be due to the prevention of Bax localization to mitochondria.

    • Enzyme delivery using protein-stabilizing and cell-penetrating 30Kc19α protein nanoparticles

      2017, Process Biochemistry
      Citation Excerpt :

      It is a member of the 30K protein family originating from the hemolymph of the silkworm, Bombyx mori. We have previously described anti-apoptotic effects in various cells via 30K gene expression or addition of recombinant 30K protein produced from Escherichia coli [18–30]. The enzyme-stabilizing and cell-penetrating effects of 30Kc19 protein have also been demonstrated [14,31,32].

    • Lysine acetylation stabilizes SP2 protein in the silkworm Bombyx mori

      2016, Journal of Insect Physiology
      Citation Excerpt :

      The hemolymph of B. mori contains many nutrient storage and immunity-related proteins, showing important functions in the growth and development of the silkworm (Li et al., 2012; Zhang et al., 2014a). Many experiments have shown that silkworm hemolymph can resist insect and mammalian cell apoptosis, demonstrating anti-apoptosis activity (Choi et al., 2002; Rhee et al., 2002; Rhee and Park, 2000), and apoptosis-inhibiting components from hemolymph have also been identified, such as storage protein (SP) and 30 K proteins (Kim et al., 2003, 2001; Rhee et al., 2007). SP2 is a member of the SP protein family that can inhibit apoptosis induced by many factors, such as staurosporine and BmNPV (Yu et al., 2013).

    View all citing articles on Scopus
    1

    To whom correspondence should addressed. Fax: +82-2-888-7295. E-mail: [email protected].

    View full text