Intracellular mannose binding lectin mediates subcellular trafficking of HIV-1 gp120 in neurons

Autor: Benchawanna Soontornniyomkij, S. Divakar, Cristian L. Achim, Marcus Kaul, C. Teodorof, Kumud K. Singh
Rok vydání: 2014
Předmět:
viruses
Mannose
Golgi Apparatus
Mannose binding lectin
HIV Envelope Protein gp120
Endoplasmic Reticulum
Microtubules
chemistry.chemical_compound
2.2 Factors relating to the physical environment
Aetiology
Cells
Cultured

Neuronal transport
Microtubule associated protein-2
Neurons
Microscopy
HIV-1 gp120
Microscopy
Confocal

Cultured
Tumor
Blotting
Nocodazole
virus diseases
Tubulin Modulators
Cell biology
Transport protein
Protein Transport
Infectious Diseases
Neurology
Confocal
symbols
HIV/AIDS
Western
Intracellular
Cells
Blotting
Western

Clinical Sciences
chemical and pharmacologic phenomena
Biology
Mannose-Binding Lectin
Article
lcsh:RC321-571
Cell Line
Subcellular trafficking
symbols.namesake
Microtubule
Cell Line
Tumor

Neurites
Humans
Immunoprecipitation
Transport Vesicles
lcsh:Neurosciences. Biological psychiatry. Neuropsychiatry
Organelles
Neurology & Neurosurgery
Endoplasmic reticulum
Neurosciences
Golgi apparatus
bacterial infections and mycoses
Good Health and Well Being
chemistry
HIV-1
Zdroj: Neurobiology of Disease, Vol 69, Iss, Pp 54-64 (2014)
Popis: Human immunodeficiency virus -1 (HIV-1) enters the brain early during infection and leads to severe neuronal damage and central nervous system impairment. HIV-1 envelope glycoprotein 120 (gp120), a neurotoxin, undergoes intracellular trafficking and transport across neurons; however mechanisms of gp120 trafficking in neurons are unclear. Our results show that mannose binding lectin (MBL) that binds to the N-linked mannose residues on gp120, participates in intravesicular packaging of gp120 in neuronal subcellular organelles and also in subcellular trafficking of these vesicles in neuronal cells. Perinuclear MBL:gp120 vesicular complexes were observed and MBL facilitated the subcellular trafficking of gp120 via the endoplasmic reticulum (ER) and Golgi vesicles. The functional carbohydrate recognition domain of MBL was required for perinuclear organization, distribution and subcellular trafficking of MBL:gp120 vesicular complexes. Nocodazole, an agent that depolymerizes the microtubule network, abolished the trafficking of MBL:gp120 vesicles, suggesting that these vesicular complexes were transported along the microtubule network. Live cell imaging confirmed the association of the MBL:gp120 complexes with dynamic subcellular vesicles that underwent trafficking in neuronal soma and along the neurites. Thus, our findings suggest that intracellular MBL mediates subcellular trafficking and transport of viral glycoproteins in a microtubule-dependent mechanism in the neurons.
Databáze: OpenAIRE