i met a problem and i've been working in campus lab to the u burke

program and we are studying h p v or human couple on the virus type

sixteen

and h p v types sixteen is the main cause of cervical cancer it causes

fifty percent of all cervical cancers each year

all the other h p v types combined account the other fifty percent

and the question we wanted to solve when it comes h p v infection

is how does invade a whole cell and set up a success one faction

and h p v is a non on the left virus and so when it

gets taken into a cell

it encounters a serious there you're to its successful infection in the form of an

in this normal member

when it gets taken in

it has to get its genome across the non polar

and is a membrane this is a difficult process because the aging on is very

pull

in order to do this the

the virus somehow has to disrupt that membrane or for a pork process

we don't know which way h p v is doing whether just completely destroying the

and dissolve or if it's forming a small or through which can get it you

know so we found this trend membrane region on that caps approaching

when we looked closer at it we found these highly conserved g x three g

motives all throughout the trans membrane domain

g extra g motifs

are

protein multi switch in which there's one nikolai seen then three of any amino acid

then another glancing

these motives of previously been shown to mediate trans membrane domain interactions within membrane so

they the question is an extremely small amino acid

so what that what these three g motif do is on alpha helix

puts the glide things right on top of each other and sense that pricing is

so small it provides almost like a slot where other trends membrane domains containing z

x three john g motifs can slide into each other in interact all so that

are l two peptide or are l two region

and then a mute of the l two that we created for the each team

you

the teaching and essentially just insert several very polar amino acids in to the middle

of the trans membrane domain which otherwise is very non polar

and what we found it is that the wild type l two trends member a

domain doesn't fact function as at remembering domain but are each d you version does

not so we now know that the

defect in

the h t mutant is that it can't escape the end result

so

we then we're and we wanted to

study more closely those d x three d motifs and how they affect this process

and so we created several alan insertion you switch unlike the h t new do

not destroy to trans membrane functionalities of this region but what it will do is

it'll throw out of key all those d x three g motifs

and what we found with those means is that

the one called eight fifty five was completely non infectious

the a sixty was slightly infectious and the a sixty four was completely normal so

this tells us the team or and terminology extra g might use are essential for

infection the more see terminal ones or not

we then went into a

we then wanted to study

what exactly those the extra g motifs are interacting with and interacting with themselves or

their interacting with some unknown factor given the way h p v works most people

clearly infection on their own

and it doesn't become a problem joe years after the actual infection process is over

it doesn't sir this peptide isn't really medically relevant

two age pvi stopping h p v infection but we hope to take that same

idea and applied to more medically relevant viruses that might use the same type of

infection system

and so

in conclusion

essentially what we found is that

h p v gets a genome across that and is normal membrane by using a

trend member a domain your the end terminus of l two which can change g

x three g maltese along which the l two protein interacts with itself and perhaps

other proteins form for that the genome can get through