Hepatitis B virus surface antigen interacts with acid alpha-glucosidase and alters glycogen metabolism

Jui Hsiang Hung, Chiao Wen Yan, Ih Jen Su, Hui Ching Wang, Huan Yao Lei, Wan Chi Lin, Wen-Tsan Chang, Wen-Ya Huang, Te Jung Lu, Ming-Derg Lai

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Aim: Hepatitis B virus (HBV) infection is highly correlated with hepatocellular carcinoma. Previous studies have reported that expression of hepatitis B virus pre-S2 mutant surface antigen is related to hepatoma development. An aberrant carbohydrate metabolism is a hallmark of malignant transformation. Methods: We performed yeast two-hybrid screening with HBV pre-S2-del large surface protein (pre-S2Δ) by using human liver cDNA library, and identified the acid alpha-glucosidase (acid α-glucosidase) as the novel cellular interacting protein of pre-S2Δ. The association of pre-S2Δ with the acid α-glucosidase was confirmed by confocal immunofluorescence and co-immunoprecipitation assay. Further, the acid α-glucosidase activity and glycogen content were analyzed in ML-1 cells expressing pre-S2Δ. Results: The interaction between HBV large surface protein and acid α-glucosidase was demonstrated with co-immunoprecipitation in vitro and in vivo, and the binding was mediated through c-terminal region 889-952 amino acid of acid α-glucosidase. On the other hand, HBV large surface protein interacted with acid α-glucosidase through N-terminal region 1-157 amino acid of HBV large surface protein. Expression of HBV large surface protein enhanced acid α-glucosidase activity and resulted in decrease of cellular glycogen. Conclusion: Our result demonstrates that HBV large surface protein interacts with acid α-glucosidase which plays an important role in glycogen balance. Together, these data suggest a novel pathway by which HBV large surface protein affects carbohydrate metabolism.

Original languageEnglish
Pages (from-to)633-640
Number of pages8
JournalHepatology Research
Volume40
Issue number6
DOIs
Publication statusPublished - 2010 Jun 1

Fingerprint

Glucosidases
alpha-Glucosidases
Hepatitis B Surface Antigens
Glycogen
Hepatitis B virus
Acids
Carbohydrate Metabolism
Immunoprecipitation
Hepatocellular Carcinoma
Amino Acids
Virus Diseases
Surface Antigens
Gene Library
Fluorescent Antibody Technique
hepatitis B virus L protein
Membrane Proteins
Yeasts
Liver

All Science Journal Classification (ASJC) codes

  • Hepatology
  • Infectious Diseases

Cite this

Hung, Jui Hsiang ; Yan, Chiao Wen ; Su, Ih Jen ; Wang, Hui Ching ; Lei, Huan Yao ; Lin, Wan Chi ; Chang, Wen-Tsan ; Huang, Wen-Ya ; Lu, Te Jung ; Lai, Ming-Derg. / Hepatitis B virus surface antigen interacts with acid alpha-glucosidase and alters glycogen metabolism. In: Hepatology Research. 2010 ; Vol. 40, No. 6. pp. 633-640.
@article{e6614eaed17e4b00bc95dfdd2d472f39,
title = "Hepatitis B virus surface antigen interacts with acid alpha-glucosidase and alters glycogen metabolism",
abstract = "Aim: Hepatitis B virus (HBV) infection is highly correlated with hepatocellular carcinoma. Previous studies have reported that expression of hepatitis B virus pre-S2 mutant surface antigen is related to hepatoma development. An aberrant carbohydrate metabolism is a hallmark of malignant transformation. Methods: We performed yeast two-hybrid screening with HBV pre-S2-del large surface protein (pre-S2Δ) by using human liver cDNA library, and identified the acid alpha-glucosidase (acid α-glucosidase) as the novel cellular interacting protein of pre-S2Δ. The association of pre-S2Δ with the acid α-glucosidase was confirmed by confocal immunofluorescence and co-immunoprecipitation assay. Further, the acid α-glucosidase activity and glycogen content were analyzed in ML-1 cells expressing pre-S2Δ. Results: The interaction between HBV large surface protein and acid α-glucosidase was demonstrated with co-immunoprecipitation in vitro and in vivo, and the binding was mediated through c-terminal region 889-952 amino acid of acid α-glucosidase. On the other hand, HBV large surface protein interacted with acid α-glucosidase through N-terminal region 1-157 amino acid of HBV large surface protein. Expression of HBV large surface protein enhanced acid α-glucosidase activity and resulted in decrease of cellular glycogen. Conclusion: Our result demonstrates that HBV large surface protein interacts with acid α-glucosidase which plays an important role in glycogen balance. Together, these data suggest a novel pathway by which HBV large surface protein affects carbohydrate metabolism.",
author = "Hung, {Jui Hsiang} and Yan, {Chiao Wen} and Su, {Ih Jen} and Wang, {Hui Ching} and Lei, {Huan Yao} and Lin, {Wan Chi} and Wen-Tsan Chang and Wen-Ya Huang and Lu, {Te Jung} and Ming-Derg Lai",
year = "2010",
month = "6",
day = "1",
doi = "10.1111/j.1872-034X.2010.00645.x",
language = "English",
volume = "40",
pages = "633--640",
journal = "Hepatology Research",
issn = "1386-6346",
publisher = "Wiley-Blackwell",
number = "6",

}

Hepatitis B virus surface antigen interacts with acid alpha-glucosidase and alters glycogen metabolism. / Hung, Jui Hsiang; Yan, Chiao Wen; Su, Ih Jen; Wang, Hui Ching; Lei, Huan Yao; Lin, Wan Chi; Chang, Wen-Tsan; Huang, Wen-Ya; Lu, Te Jung; Lai, Ming-Derg.

In: Hepatology Research, Vol. 40, No. 6, 01.06.2010, p. 633-640.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Hepatitis B virus surface antigen interacts with acid alpha-glucosidase and alters glycogen metabolism

AU - Hung, Jui Hsiang

AU - Yan, Chiao Wen

AU - Su, Ih Jen

AU - Wang, Hui Ching

AU - Lei, Huan Yao

AU - Lin, Wan Chi

AU - Chang, Wen-Tsan

AU - Huang, Wen-Ya

AU - Lu, Te Jung

AU - Lai, Ming-Derg

PY - 2010/6/1

Y1 - 2010/6/1

N2 - Aim: Hepatitis B virus (HBV) infection is highly correlated with hepatocellular carcinoma. Previous studies have reported that expression of hepatitis B virus pre-S2 mutant surface antigen is related to hepatoma development. An aberrant carbohydrate metabolism is a hallmark of malignant transformation. Methods: We performed yeast two-hybrid screening with HBV pre-S2-del large surface protein (pre-S2Δ) by using human liver cDNA library, and identified the acid alpha-glucosidase (acid α-glucosidase) as the novel cellular interacting protein of pre-S2Δ. The association of pre-S2Δ with the acid α-glucosidase was confirmed by confocal immunofluorescence and co-immunoprecipitation assay. Further, the acid α-glucosidase activity and glycogen content were analyzed in ML-1 cells expressing pre-S2Δ. Results: The interaction between HBV large surface protein and acid α-glucosidase was demonstrated with co-immunoprecipitation in vitro and in vivo, and the binding was mediated through c-terminal region 889-952 amino acid of acid α-glucosidase. On the other hand, HBV large surface protein interacted with acid α-glucosidase through N-terminal region 1-157 amino acid of HBV large surface protein. Expression of HBV large surface protein enhanced acid α-glucosidase activity and resulted in decrease of cellular glycogen. Conclusion: Our result demonstrates that HBV large surface protein interacts with acid α-glucosidase which plays an important role in glycogen balance. Together, these data suggest a novel pathway by which HBV large surface protein affects carbohydrate metabolism.

AB - Aim: Hepatitis B virus (HBV) infection is highly correlated with hepatocellular carcinoma. Previous studies have reported that expression of hepatitis B virus pre-S2 mutant surface antigen is related to hepatoma development. An aberrant carbohydrate metabolism is a hallmark of malignant transformation. Methods: We performed yeast two-hybrid screening with HBV pre-S2-del large surface protein (pre-S2Δ) by using human liver cDNA library, and identified the acid alpha-glucosidase (acid α-glucosidase) as the novel cellular interacting protein of pre-S2Δ. The association of pre-S2Δ with the acid α-glucosidase was confirmed by confocal immunofluorescence and co-immunoprecipitation assay. Further, the acid α-glucosidase activity and glycogen content were analyzed in ML-1 cells expressing pre-S2Δ. Results: The interaction between HBV large surface protein and acid α-glucosidase was demonstrated with co-immunoprecipitation in vitro and in vivo, and the binding was mediated through c-terminal region 889-952 amino acid of acid α-glucosidase. On the other hand, HBV large surface protein interacted with acid α-glucosidase through N-terminal region 1-157 amino acid of HBV large surface protein. Expression of HBV large surface protein enhanced acid α-glucosidase activity and resulted in decrease of cellular glycogen. Conclusion: Our result demonstrates that HBV large surface protein interacts with acid α-glucosidase which plays an important role in glycogen balance. Together, these data suggest a novel pathway by which HBV large surface protein affects carbohydrate metabolism.

UR - http://www.scopus.com/inward/record.url?scp=77954372870&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77954372870&partnerID=8YFLogxK

U2 - 10.1111/j.1872-034X.2010.00645.x

DO - 10.1111/j.1872-034X.2010.00645.x

M3 - Article

VL - 40

SP - 633

EP - 640

JO - Hepatology Research

JF - Hepatology Research

SN - 1386-6346

IS - 6

ER -