VAMP3

Last update 08 May 2025

Basic Info

Synonyms

CEB, Cellubrevin, SYB3

+ [5]

Introduction

SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network.

100 Clinical Results associated with VAMP3

100 Translational Medicine associated with VAMP3

0 Patents (Medical) associated with VAMP3

373

Literatures (Medical) associated with VAMP3

08 Apr 2025·Infection and Immunity

Entamoeba gingivalis induces gingival cell death, collagen breakdown, and host immune response via VAMP8/-3-driven exocytosis pathways

Article

Author: Schaefer, Arne S. ; Adam, Aysegül ; Neumann, Nico ; Bao, Xin ; Rosenfeld, Lea

ABSTRACT The protozoan Entamoeba gingivalis commonly colonizes anaerobic periodontal pockets, induces a severe innate immune response, invades gingival mucosa, and kills epithelial cells. E. gingivalis infection is associated with the common oral inflammatory disease periodontitis. DNA variants in vesicle-associated membrane proteins (VAMP) -3 and -8 genes are linked to increased periodontitis risk. These genes mediate host–pathogen interactions, including mucin exocytosis to form protective barriers and matrix metalloproteinase (MMP) secretion in intestinal amoebiasis caused by Entamoeba histolytica . This study aimed to investigate the roles of VAMP3/8 in gingival defense and E. gingivalis infection mechanisms. Clustered regularly interspaced short palindromic repeats (CRISPR)-Cas9 gene editing was used to create VAMP3/8-deficient gingival epithelial cells and fibroblasts. Functional analyses included immunofluorescence, enzyme-linked immunosorbent assay (ELISA), cytotoxicity, and collagenase assays. VAMP8 co-localized with mucins in gingival epithelial cells (gECs), and VAMP3 with MMPs in gingival fibroblasts. In gECs , E. gingivalis infection increased mucin (MUC1: 3.6×, MUC21: 14.4×) and interleukin secretion (IL-8, IL-1B: >6×, P = 0.019). VAMP8 deficiency in gECs caused higher cell death (35% vs 4% in controls) with reduced exocytosis of mucins and interleukins. Likewise, E. gingivalis -induced VAMP8 translocation into lipid rafts was lost in VAMP8 knockout cells, validating the participation of VAMP8 in exocytosis. In wild-type but not VAMP3-deficient gingival fibroblasts, E. gingivalis strongly activated collagenases. E. gingivalis effects were more pathogenic than those of the oral anaerobic bacterium Porphyromonas gingivalis. E. gingivalis exploits VAMP8/3-driven exocytosis pathways, driving inflammation and tissue destruction, underscoring its role as a significant periodontal pathogen.

01 Apr 2025·Biophysical Journal

SNARE complex assembly and disassembly dynamics in response to Ca2+ current activation in live cells

Article

Author: Fang, Qinghua ; Zhao, Ying ; An, Dong ; Lindau, Manfred

A SNAP25-based FRET construct named SCORE (SNARE complex reporter) has revealed a transient FRET increase that specifically occurred at fusion sites preceding fusion events by tens of milliseconds and presumably reflects vesicle priming. The FRET increase lasts for a few seconds until it is reversed. In those experiments, the FRET increase was found to be localized to areas <0.5 μm² at sites of transmitter release as detected amperometrically using electrochemical detector arrays. Due to the localization to such small areas, it was unknown if the reversal of the FRET increase is due to local dispersion of high-FRET SCORE copies leaving the site after fusion and exchange with surrounding low-FRET copies, or if it reflects disassembly of the high-FRET complexes. To resolve this question, we performed whole-cell patch-clamp pulse stimulation experiments, imaging the entire footprint of the cells in total internal reflection fluorescence (TIRF) excitation mode such that diffusional exchange between high-FRET and low-FRET copies does not produce a net FRET change. We show here that pulse stimulation of calcium currents results in FRET ratio transients with a time course very similar to those related to fusion events. By comparing the kinetics of the FRET ratio decay with analytical and numerical diffusion simulation results, we show that the experimentally observed kinetics cannot be explained by diffusional exchange and conclude that the SCORE FRET ratio transients reflect incorporation of SCORE in SNARE complexes followed by SNARE complex disassembly. Experiments using Synaptobrevin 2/Cellubrevin double knockout mouse embryonal chromaffin cells showed no pulse-induced FRET change, indicating that the vSNARE is required for the incorporation of SCORE (or SNAP25 in wild-type cells) in the SNARE complex during priming.

12 Mar 2025·mBio

Rickettsial pathogen augments tick vesicular-associated membrane proteins for infection and survival in the vector host

Article

Author: Sultana, Hameeda ; Patel, Avni ; Kolape, Jaydeep ; Neelakanta, Girish ; Namjoshi, Prachi

ABSTRACTAnaplasma phagocytophilum is an obligate intracellular rickettsial pathogen that infects humans and animals. The black-legged tick Ixodes scapularis acts as a vector and transmits this bacterium to the vertebrate host. Upon entry into a host cell, A. phagocytophilum resides and multiplies in a host-derived vacuole called morulae. There is not much information available on the molecules that play an important role(s) in A. phagocytophilum entry and formation of these morulae in tick cells. In this study, we provide evidence that tick vesicular-associated membrane proteins, VAMP3 and VAMP4, play important roles in this phenomenon. Quantitative real-time polymerase chain reaction (QRT-PCR) analysis showed that both vamp3 and vamp4 transcripts are significantly upregulated at early time points of A. phagocytophilum infection in tick cells. We noted that both VAMP3 and VAMP4 predominantly localized to the A. phagocytophilum -containing vacuole. RNAi-mediated silencing of vamp3 and/or vamp4 expression, followed by confocal microscopy and expression analysis, indicated an impairment in A. phagocytophilum morulae formation in tick cells. We also noted that VAMP3 and VAMP4 play a role in the A. phagocytophilum persistent infection of ticks and tick cells. Furthermore, RNAi-mediated silencing of expression of arthropod vamp3 and vamp4 affected bacterial acquisition from an infected murine host to ticks. Collectively, this study not only provides evidence on the role of arthropod vesicular-associated membrane proteins in A. phagocytophilum morulae formation in tick cells but also demonstrates that these proteins are important for bacterial acquisition from an infected vertebrate host into ticks. IMPORTANCEAnaplasma phagocytophilu m is a tick-borne pathogen primarily transmitted by black-legged Ixodes scapularis ticks to humans and animals. This bacterium enters host cells, forms a host-derived vacuole, and multiplies within this vacuole. The molecules that are critical in the formation of host-derived vacuole in tick cells is currently not well-characterized. In this study, we provide evidence that arthropod vesicular-associated membrane proteins, VAMP3 and VAMP4, are critical for A. phagocytophilum early and persistent infection in tick cells. These arthropod proteins are important for the formation of host-derived vacuoles in tick cells. Our study also provides evidence that these proteins are important for A. phagocytophilum acquisition from the infected murine host into ticks. Characterization of tick molecules important in bacterial entry and/or survival in the vector host could lead to the development of strategies to target this and perhaps other rickettsial pathogens.

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VAMP3

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