Page 109 - Avian Virology: Current Research and Future Trends

102 | Paldurai and Samal

Table 3.5 Continued
Fusion protein features
Potential Potential disulfide
APMV Signal Fusion N-glycosylation bonded cysteine
serotype F0 F2 F1 peptide a peptide b HRA c HRB c TM d CT d sites e residues f
APMV-19 536 1–105 106–536 1–19 106–130 134–184 451–484 490–513 514–536 74, 94, 180, 436, 4–390, 65–188,
460, 481 327–351, 336–413,
359–383, 388–508
APMV-20 537 1–101 102–537 1–20 102–126 127–173 446–477 485–509 510–537 61, 74, 456, 483 20–323, 65–227,
184–490, 332–409,
347–386, 355–379,
384–508
APMV-21 i 551 1–111 112–551 1–24 112–136 138–183 457–507 495–519 520–551 80, 186, 361, 466 71–194, 333–357,
342–419, 365–389,
394–518
a Signal peptide sequence was predicted using SignalP 4.1 Server (Petersen et al., 2011; Nielsen, 2017).
b After the precursor F protein (F0) cleavage, first 25 hydrophobic amino acid sequence form the fusion peptide at the N-terminus of the F1 subunit.
c Heptad repeat regions A and B (HRA and HRB, respectively) were predicted using LearnCoil-VMF program (Berger and Singh, 1997; Singh et al.,
1999).
d The transmembrane (TM) and the cytoplasmic tail (CT) domains of the F protein were predicted using HMMTOP 2.0 server (Tusnády and Simon,
1998, 2001).
e Potential N-glycosylation sites were predicted using NetNGlyc 1.0 Server (Gupta et al., 2004). The Arabic numerals indicate positions of Asn (N)
residues in the F protein that has the potential for glycosylation.
f Potential disulphide bonded Cysteine residues were predicted using DiANNA 1.1 web server (Ferrè and Clote, 2005a,b, 2006). The hyphenated
Arabic numerals indicate the positions of disulphide bonded Cysteine residues in the F protein.
g The fusion (F) protein features of APMV-2 is diagrammatically represented in the Fig. 3.9A.
h The signal peptide sequence was only suggested but not predicted by SignalP 4.1 Server (Petersen et al., 2011; Nielsen, 2017).
i Putative APMV serotype awaiting official recognition from the ICTV.
Table 3.6 Haemagglutinin-neuraminidase protein features of APMV serotypes
HN protein features
APMV
serotype HN length CT a TM a HN ectodomain a Potential N-glycosylation sites b
APMV-1 577 1–26 27–45 46–577 119, 341, 433
APMV-2 c 580 1–25 26–44 45–580 279, 346, 391
APMV-3 577 1–26 27–46 47–577 32, 57, 122, 312, 325, 383, 502
APMV-4 569 1–27 28–46 47–569 11, 58, 141, 317, 448
APMV-5 574 1–20 21–39 40–574 58, 119, 148, 278, 346, 383
APMV-6 613 1–30 31–49 50–613 125, 284, 352, 383, 495
APMV-7 569 1–14 15–37 38–569 48, 109, 135, 268, 333, 367, 482, 511, 562
APMV-8 577 1–26 27–45 46–577 121, 280, 515
APMV-9 579 1–26 27–44 45–579 147, 341, 348, 433
APMV-10 575 1–26 27–44 45–575 121, 149, 280, 352, 489
APMV-11 583 1–25 26–47 48–583 148, 151, 279, 327, 346, 492, 497
APMV-12 614 1–26 27–45 46–614 147, 341, 348
APMV-13 610 1–26 27–45 46–610 119, 341, 392, 604
APMV-14 580 1–25 26–45 46–580 119, 148, 266, 278, 346, 377
APMV-15 579 1–28 29–47 48–579 2, 13, 157, 282, 336, 432
APMV-16 618 1–26 27–46 47–618 341, 508, 602
APMV-17 599 1–57 58–75 76–599 150, 379, 425, 464, 477, 547
APMV-18 579 1–34 35–52 53–579 127, 152, 274, 356, 454, 521
APMV-19 587 1–27 28–46 47–587 120, 342, 395, 434, 514, 581
APMV-20 578 1–28 29–49 50–578 51, 123, 150, 169, 282, 351, 387, 491, 548
APMV-21 d 567 1–26 27–51 52–567 147, 341, 348, 433, 500
a The cytoplasmic tail (CT), the transmembrane (TM) and the ectodomains of the HN protein were predicted using HMMTOP 2.0 server (Tusnády
and Simon, 1998, 2001).
b Potential N-glycosylation sites were predicted using NetNGlyc 1.0 Server (Gupta et al., 2004). The Arabic numerals indicate positions of Asn (N)
residues in the HN protein that has the potential for glycosylation.
c The hemagglutinin-neuraminidase (HN) protein features of APMV-2 is diagrammatically represented in Fig. 3.9B.
d Putative APMV serotype awaiting official recognition from the ICTV.