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Am J Transl Res 2013;5(6):634-642
Original Article
Mycoplasma hyorhinis markedly degrades β-amyloid peptides in vitro
and ex vivo: a novel biological approach for treating Alzheimer’s
disease?
Ahsan Habib, Juan Deng, Huayan Hou, Qiang Zou, Brian Giunta, Yan-Jiang Wang, Demian Obregon, Darrell
Sawmiller, Song Li, Takashi Mori, Jun Tan
Rashid Laboratory for Developmental Neurobiology, Silver Child Development Center, Morsani College of
Medicine, University of South Florida, Tampa, Florida 33613; Neuroimmunology Laboratory, Morsani College of
Medicine, University of South Florida, Tampa, Florida 33613; Department of Neurology, Daping Hospital, The
Third Military Medical University, Chongqing 42000, China; Department of Biophysics, School of Physics and
Optoelectronic Technology, Dalian University of Technology, Dalian, China; Departments of Biomedical Sciences
and Pathology, Saitama Medical Center and University, Kawagoe, Saitama, 350-8550, Japan
Received August 16, 2013; Accepted September 3, 2013; Epub September 25, 2013; Published September 30,
2013
Abstract: Accumulation of amyloid-β (Aβ) peptides (predominantly Aβ40, 42) and their aggregation into plaques
in the brain are thought to be the one of the major causes of Alzheimer’s disease (AD). Originally discovered in
our Chinese hamster ovary (CHO) cell line stably expressing human wild-type amyloid precursor protein (APP)
(CHO/APPwt) cultures devoid of Aβ production, we found that Mycoplasma selectively degrades soluble Aβ in a
time and dose (colony forming unit) dependent manner. Moreover, we fully characterized the Mycoplasma species
as Mycoplasma hyorhinis (M. hyorhinis) by genetic and colony morphological analyses by light microscopy. Most
interestingly, we attenuated the pathogenicity of M. hyorhinis by γ irradiation (3.5 Gy), and found that its ability to
degrade Aβ was retained. On the other hand, heated and sonicated M. hyorhinis failed to retain this ability to
degrade Aβ, suggesting that this degradation requires viable cells and likely a biologically active signaling
pathway. In addition, we found that M. hyorhinis can degrade Aβ produced in AD model mice (PSAPP mice) ex
vivo. Finally, we found that irradiated (non-pathogenic) M. hyorhinis also can degrade Aβ produced in PSAPP mice
in vivo. These studies suggest that irradiated (non-pathogenic) M. hyorhinis can be a novel and alternative
biological strategy for AD treatment. (AJTR1308006).
Keywords: Mycoplasma, Alzheimer’s disease, amyloid-β peptide, amyloid precursor protein
Address correspondence to: Jun Tan, Rashid Laboratory for Developmental Neurobiology, Silver Child
Development Center, Morsani College of Medicine, University of South Florida, 3515 E. Fletcher Ave., Tampa,
Florida 33613. Tel: 813-974-9326; E-mail: jtan@health.usf.edu
Original Article
Mycoplasma hyorhinis markedly degrades β-amyloid peptides in vitro
and ex vivo: a novel biological approach for treating Alzheimer’s
disease?
Ahsan Habib, Juan Deng, Huayan Hou, Qiang Zou, Brian Giunta, Yan-Jiang Wang, Demian Obregon, Darrell
Sawmiller, Song Li, Takashi Mori, Jun Tan
Rashid Laboratory for Developmental Neurobiology, Silver Child Development Center, Morsani College of
Medicine, University of South Florida, Tampa, Florida 33613; Neuroimmunology Laboratory, Morsani College of
Medicine, University of South Florida, Tampa, Florida 33613; Department of Neurology, Daping Hospital, The
Third Military Medical University, Chongqing 42000, China; Department of Biophysics, School of Physics and
Optoelectronic Technology, Dalian University of Technology, Dalian, China; Departments of Biomedical Sciences
and Pathology, Saitama Medical Center and University, Kawagoe, Saitama, 350-8550, Japan
Received August 16, 2013; Accepted September 3, 2013; Epub September 25, 2013; Published September 30,
2013
Abstract: Accumulation of amyloid-β (Aβ) peptides (predominantly Aβ40, 42) and their aggregation into plaques
in the brain are thought to be the one of the major causes of Alzheimer’s disease (AD). Originally discovered in
our Chinese hamster ovary (CHO) cell line stably expressing human wild-type amyloid precursor protein (APP)
(CHO/APPwt) cultures devoid of Aβ production, we found that Mycoplasma selectively degrades soluble Aβ in a
time and dose (colony forming unit) dependent manner. Moreover, we fully characterized the Mycoplasma species
as Mycoplasma hyorhinis (M. hyorhinis) by genetic and colony morphological analyses by light microscopy. Most
interestingly, we attenuated the pathogenicity of M. hyorhinis by γ irradiation (3.5 Gy), and found that its ability to
degrade Aβ was retained. On the other hand, heated and sonicated M. hyorhinis failed to retain this ability to
degrade Aβ, suggesting that this degradation requires viable cells and likely a biologically active signaling
pathway. In addition, we found that M. hyorhinis can degrade Aβ produced in AD model mice (PSAPP mice) ex
vivo. Finally, we found that irradiated (non-pathogenic) M. hyorhinis also can degrade Aβ produced in PSAPP mice
in vivo. These studies suggest that irradiated (non-pathogenic) M. hyorhinis can be a novel and alternative
biological strategy for AD treatment. (AJTR1308006).
Keywords: Mycoplasma, Alzheimer’s disease, amyloid-β peptide, amyloid precursor protein
Address correspondence to: Jun Tan, Rashid Laboratory for Developmental Neurobiology, Silver Child
Development Center, Morsani College of Medicine, University of South Florida, 3515 E. Fletcher Ave., Tampa,
Florida 33613. Tel: 813-974-9326; E-mail: jtan@health.usf.edu
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