'''Lateral bodies''' are structures that sit on the concave sides of the viral core of a poxvirus and is surrounded by a membrane.<ref>{{Cite journal |last=Bidgood |first=Susanna R. |date=2019-01-30 |title=Continued poxvirus research: From foe to friend |journal=PLOS Biology |language=en |volume=17 |issue=1 |article-number=e3000124 |doi=10.1371/journal.pbio.3000124 |issn=1545-7885 |pmc=6370227 |pmid=30699104 |doi-access=free }}</ref> They serve as immunomodulatory delivery packets, and membrane cloaking to spread poxviruses.<ref>{{Cite journal |last1=Bidgood |first1=Susanna R. |last2=Mercer |first2=Jason |date=2015-08-21 |title=Cloak and Dagger: Alternative Immune Evasion and Modulation Strategies of Poxviruses |journal=Viruses |volume=7 |issue=8 |pages=4800–4825 |doi=10.3390/v7082844 |issn=1999-4915 |pmc=4576205 |pmid=26308043|doi-access=free }}</ref> They were first visualized using electron microscopy in 1956 and shortly after, it was shown that they detach from the viral core upon membrane fusion.<ref>{{Cite journal |last=Peters |first=D. |date=1956-12-29 |title=Morphology of resting vaccinia virus |journal=Nature |volume=178 |issue=4548 |pages=1453–1455 |doi=10.1038/1781453a0 |issn=0028-0836 |pmid=13387736|bibcode=1956Natur.178.1453P |s2cid=2136476 |doi-access=free }}</ref><ref>{{Cite journal |last=Dales |first=Samuel |title=The uptake and development of vaccinia virus in strain L cells followed with labeled viral deoxyribonucleic acid |date=1963-07-01 |journal=The Journal of Cell Biology |volume=18 |issue=1 |pages=51–72 |doi=10.1083/jcb.18.1.51 |issn=0021-9525 |pmc=2106286 |pmid=14024720}}</ref>
== Lateral body proteins == Lateral bodies are made up of at least three proteins, phosphoprotein F17, dual-specificity phosphatase H1 and the viral oxidoreductase G4.<ref name=":0">{{Cite journal |last1=Schmidt |first1=Florian Ingo |last2=Bleck |first2=Christopher Karl Ernst |last3=Reh |first3=Lucia |last4=Novy |first4=Karel |last5=Wollscheid |first5=Bernd |last6=Helenius |first6=Ari |last7=Stahlberg |first7=Henning |last8=Mercer |first8=Jason |date=2013-08-15 |title=Vaccinia virus entry is followed by core activation and proteasome-mediated release of the immunomodulatory effector VH1 from lateral bodies |journal=Cell Reports |volume=4 |issue=3 |pages=464–476 |doi=10.1016/j.celrep.2013.06.028 |issn=2211-1247 |pmid=23891003|s2cid=27275011 |doi-access=free |hdl=20.500.11850/70158 |hdl-access=free }}</ref> F17 is the main structural protein and may play a role in modulating cellular immune response through MAPK signaling pathways.<ref>{{Cite journal |last1=Wickramasekera |first1=Nadi T. |last2=Traktman |first2=Paula |date=July 2010 |title=Structure/Function Analysis of the Vaccinia Virus F18 Phosphoprotein, an Abundant Core Component Required for Virion Maturation and Infectivity |journal=Journal of Virology |volume=84 |issue=13 |pages=6846–6860 |doi=10.1128/JVI.00399-10 |issn=0022-538X |pmc=2903294 |pmid=20392848}}</ref> H1 dephosphorylates STAT1 to prevent nuclear transcription and block IFNy-induced immune signaling.<ref name=":0" /> Finally, G4 is essential for viral morphogenesis.<ref name=":0" /> Additionally, the proteins packed in lateral bodies are redox proteins, which modulates the host oxidative response impacting early gene expression and virion production.<ref>{{Cite journal|vauthors=Bidgood SR, Samolej J, Novy K, Collopy A, Albrecht D, Krause M, Burden JJ, Wollscheid B, Mercer J|date=14 July 2022 |title=Poxviruses package viral redox proteins in lateral bodies and modulate the host oxidative respons |journal=PLOS Pathog|volume=18|issue=7|article-number=e1010614|pmid=35834477|pmc=9282662|doi=10.1371/journal.ppat.1010614|doi-access=free}}</ref>
== References == {{reflist}}
Category:Viruses