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<i>Trimeresurus nebularis</i> is a montane pit viper that causes bites and envenomation to various communities in the central highland region of Malaysia, in particular Cameron&#8217;s Highlands. To unravel the venom composition of this species, the venom proteins were digested by trypsin and subjected to nano-liquid chromatography-tandem mass spectrometry (LC-MS/MS) for proteomic profiling. Snake venom metalloproteinases (SVMP) dominated the venom proteome by 48.42% of total venom proteins, with a characteristic distribution of P-III: P-II classes in a ratio of 2:1, while P-I class was undetected. Snaclecs constituted the second most venomous protein family (19.43%), followed by snake venom serine proteases (SVSP, 14.27%), phospholipases A₂ (5.40%), disintegrins (5.26%) and minor proteins including cysteine-rich secretory proteins, L-amino acid oxidases, phosphodiesterases, 5&#8242;-nucleotidases. The venomic profile correlates with local (painful progressive edema) and systemic (hemorrhage, coagulopathy, thrombocytopenia) manifestation of <i>T. nebularis</i> envenoming. As specific antivenom is unavailable for <i>T. nebularis</i>, the hetero-specific Thai Green Pit viper Monovalent Antivenom (GPVAV) was examined for immunological cross-reactivity. GPVAV exhibited good immunoreactivity to <i>T. nebularis</i> venom and the antivenom effectively cross-neutralized the hemotoxic and lethal effects of <i>T. nebularis</i> (lethality neutralizing potency = 1.6 mg venom per mL antivenom). The findings supported GPVAV use in treating <i>T. nebularis</i> envenoming.