Table 2.

A summary of various critical functions performed by various EBOV proteins and their amino acids involved.

Protein	Amino Acids (aa)	Function	Reference
NP	1–450, especially 160, 171, 174, 298, 310 and 401	RNA encapsidation/ssRNA binding	[12,13,88]
	1–450, especially 110, 349, 373, 374, 382 and 383	NP oligomerization; significant for nucleocapsid (NC) formation	[13,87,89]
	1–450 (especially 244–383, critically 240, 248 and 252) and 481–500	NP-VP35 interaction; significant for viral RNA synthesis regulation	[88,90]
	2–150 and 601–739	NP-VP40 interaction; significant for recruiting NP into VLP	[95]
	562–567	NP-PP2A-B56 phosphatase interaction; significant for enabling viral transcription	[99]
	581–591	Recruiting host SET and MYND domain-containing protein 3 (SMYD3); significant for viral transcription regulation	[100]
	600–617	NP-VP30 interaction; significant for viral RNA transcription	[96,97]
	641–739	Inclusion body and virus-like particle (VLP) formation	[92]
VP35	20–48, 225, 248 and 251	VP35-NP interaction; significant for viral RNA synthesis regulation	[88,104]
	82–118	VP35 homo-oligomerization; significant for VP35-L interaction	[105]
	221–340, especially 239, 312 and 322	Interaction with protein activator of IFN-induced protein kinase (PACT); significant to prevent activation of PACT-induced RIG-I ATPase	[106]
	225, 248, 251, 282, 283, 298 and 300	Enable VP35 to function as a non-enzymatic co-factor for the L protein	[104,107]
	304–340	Inactivating protein kinase R (PKR); significant for continuous viral protein synthesis	[108]
	305, 309, 312, 319, 322 and 339	Binding to dsRNA; significant to protect dsRNA from recognition by host immune receptors	[107,109,110]
VP40	52–65, 95, 108–117 and 160	VP40 dimerization; significant for VP40 cellular trafficking	[111,112]
	125 and 134	Octameric VP40 and ssRNA binding; significant for negative transcription regulation	[112,113]
	127, 129, 130 and 212–214	Significant for VP40 localization to the plasma membrane, oligomerization and budding	[114,115]
	221, 224, 225, 270, 274 and 275	VP40 interaction with plasma membrane	[112]
	241 and 307	VP40 filaments formation; significant for assembly and budding	[112]
	292–295	Significant for VLP production and controlled viral transcription inhibition	[116]
	303–307	VP40-Sec24C interaction; significant for internal trafficking of VP40 to plasma membrane	[82]
GP	43, 52, 54, 56, 57, 60, 61, 63, 64, 66, 79, 82, 88, 95, 114, 115, 140, 143, 146, 147, 153, 154, 159, 170 and 181	Significant for viral entry	[117,118,119,120,121]
	54–201	Receptor-binding site	[122]
	55, 57, 63 and 64	Involved in membrane fusion-mediated conformational changes	[123]
	159, 160, 162, 170 and 214–270	GP stability	[119,120]
	190–213, especially aa 190, 193 and 194	Cathepsin cleavage site; significant for viral interaction with the obligate host receptor	[123,124]
	529, 531, 533, 534, 535 and 537	Hydrophobic residues which insert into the target cell membrane	[123]
	563 and 618	2 N-linked glycosylation sites; significant for GP processing, oligomerization and functioning	[75,125]
	585–609	Immunosuppressive motif; cause lymphocyte apoptosis and cytokine dysregulation.	[29,31,126]
VP30	27–40	VP30-ssRNA interaction	[127]
	68–95	Zinc-binding site; significant for transcription regulation	[128]
	140–266	VP30-NP interaction; significant for viral transcription	[96,97,129]
	179, 180 and 183	Significant for transcription initiation	[129]
VP24	96–98 and 106–121	VP24-unphosphorylated STAT1 interaction	[130,131]
	115, 121, 124, 125, 128–131, 135, 137, 138, 140, 184–186, 201, 203–205 and 207	VP24-KPNA5 interaction	[131]
	142–147 and 26–50, especially 36–45	VP24-KPNA1 interaction	[132]
	169–173, critically 170 and 171	VP24-NP interaction; significant for NC formation and viral replication	[133]