Fig 1.
Molecular model of biological assembly of HAdV-D10 is shown in cartoon style in panel A with a colour key highlighting protein components. Panels B and C show rotated views of the modelled asymmetric unit that repeats to form the biological assembly. Shown are exterior (B), and interior (C) capsid views respectively displaying modelled major proteins hexon and penton and minor proteins IIIa, VIII, VI and IX.
Fig 2.
Panel A presents a focused refinement cryo-EM map of major protein fiber at 4.6 Å resolution with an AlphaFold3 predicted model of the trimeric fiber shaft and pentameric penton fitted into the map. The AlphaFold model is coloured by standard pLDDT confidence scores colours dark blue >90, light blue 90 - 70, yellow 70 - 50 and orange <50. Fiber ‘umbrella’ motif is highlighted with a dotted box. Panel B a top down view of the fiber protein illustrating the fiber knob. Panel C shows view of fiber motif with rainbow colour scheme to illustrate fold. N- termini to C-termini residues are coloured blue, cyan, green, yellow then red. Hydrophobic colouring and surface representation of fiber motif are presented in panel D. Coulombic colouring and surface representation of fiber motif are shown in panel E illustrating electrostatic properties of residues. Panel F sequence of umbrella motif residues 111-161 with charged residues coloured and secondary structure elements labelled and coloured by N- to C- termini rainbow colour scheme as in panel C.
Fig 3.
Comparison of HAdV Fiber Shaft Structures.
Panel A presents sequence analysis of fiber shafts after structural alignment to umbrella motif residues 111-161 of HAdV-D10. Panel B presents a comparison of AlphaFold3 modelled structures of HAdV fiber shafts coloured by standard pLDDT confidence scores, colour key displayed. Comparison of shaft structures shows species D serotypes HAdV-D10 and HAdV-D26 have similar sequence identity and the umbrella motif predicted.
Fig 4.
Transcription map of HAdV-D10 across multiple timepoints.
Images were made in IGV [28–30]. Panel A presents an overview of the classical HAdV-C5 transcriptome map with key genes highlighted. Panel B presents the HAdV-D10 genome which the following panels are aligned to. Transcript maps with the most abundant transcript for each of the known HAdV-D10 proteins are presented for 6 hours post infection (panel C), 24 hours post infection (panel D), 48 hours post infection (panel E) and 72 hours post infection (panel F). All transcripts are grouped according to strand, with forward strand coded transcripts shown in black and reverse strand coded transcripts shown in blue. Exons are presented as rectangles, and introns as lines, with arrows highlighting the direction of the strand.
Fig 5.
Change in transcription of known HAdV-D10 genes over 24-, 48- and 72-hours post infection.
The percentage of total transcripts for each known HAdV-D10 gene are shown across the three timepoints, with values for 24 h.p.i. shown in pink, 48 h.p.i. shown in black and 72 h.p.i. shown in blue. Transcripts encoding L2_preVII or L2_VII_bysplicing have been highlighted with asterisks.
Fig 6.
Production of preVII and pVII transcripts by HAdV-D10.
Panel A illustrates HAdV-D10’s preVII and pVII transcripts observed in IGV [28–30]. The transcript equivalent to mature pVII is shown first, with preVII underneath. Panel B presents the sequences of the two different transcripts, aligned by Clustal Omega [31]. The cleavage site of the adenovirus protease is displayed for both of the sequences. Panel C presents the ratio of precursor to mature equivalent pVII transcripts at 24, 48 and 72 h.p.i.
Table 1.
Hypothetical transcripts produced by HAdV-D10 infected cells identified by NCBI BLAST [33]. Three hypothetical transcripts previously reported in NCBI Gene were identified via BLAST searching unknown transcripts. Their relative abundance has been combined for all three timepoints (labelled Transcript Abundance) and the Accession IDs associated with the hypothetical transcripts have been reported.