Journal of the American Chemical SocietyDOI: 10.1021/jacs.1c05501
Hongxiang Wu, Yiwei Zhang, Yuanxin Li, Jianchao Xu, Yu Wang, and Xuechen Li
https://ift.tt/3q2Iixy
The receptor‐binding domain (RBD) of SARS‐CoV‐2 spike glycoprotein can be prepared by semi‐synthesis as a homogeneous glycoform. In their Research Article (DOI: 10.1002/anie.202100543), Ping Wang et al. report the inaugural synthesis of glycosylated RBDs bearing structurally defined glycans. The cover picture illustrates the combination of carbohydrate and protein chemistry leading to the successful synthesis of this protein.
https://ift.tt/3aEDw2T
The first chemical synthesis of homogeneous glycoforms of the SARS‐CoV‐2 spike receptor‐binding domain (RBD) has been accomplished via the combination of protein and carbohydrate chemistry. This strategy provides a versatile synthetic platform for homogeneous glycosylated RBDs of the SARS‐CoV‐2 S protein and other related virus proteins and a powerful tool for investigating the functions of RBD glycans.
Abstract
SARS‐CoV‐2 attaches to its host receptor, angiotensin‐converting enzyme 2 (ACE2), via the receptor‐binding domain (RBD) of the spike protein. The RBD glycoprotein is a critical target for the development of neutralizing antibodies and vaccines against SARS‐CoV‐2. However, the high heterogeneity of RBD glycoforms may lead to an incomplete neutralization effect and impact the immunogenic integrity of RBD‐based vaccines. Investigating the role of different carbohydrate domains is of paramount importance. Unfortunately, there is no viable method for preparing RBD glycoproteins with structurally defined glycans. Herein we describe a highly efficient and scalable strategy for the preparation of six glycosylated RBDs bearing defined structure glycoforms at T323, N331, and N343. A combination of modern oligosaccharide, peptide synthesis and recombinant protein engineering provides a robust route to decipher carbohydrate structure‐function relationships.
https://ift.tt/30CAAhI
Journal of the American Chemical SocietyDOI: 10.1021/jacs.0c08719
Yuta Maki, Ryo Okamoto, Masayuki Izumi, and Yasuhiro Kajihara
https://ift.tt/3fuAHCF
Journal of the American Chemical SocietyDOI: 10.1021/jacs.0c12448
Hongxing Li, Jun Zhang, Chuanjing An, and Suwei Dong
https://ift.tt/3pgiBYi
Uncovering stability of DC‐SIGN glycoforms with native mass spectrometry : A combined strategy of exoglycosidase sequencing, native mass spectrometry, ion mobility, and gas‐phase unfolding uncovered the occupancy and structural detail of O‐glycans present on the carbohydrate binding domain of DC‐SIGN. Collision‐induced unfolding by ion mobility revealed differences in stability among glycoforms, independent of glycoprotein mass.
Abstract
The immune scavenger protein DC‐SIGN interacts with glycosylated proteins and has a putative role in facilitating viral infection. How these recognition events take place with different viruses is not clear and the effects of glycosylation on the folding and stability of DC‐SIGN have not been reported. Herein, we report the development and application of a mass‐spectrometry‐based approach to both uncover and characterise the effects of O‐glycans on the stability of DC‐SIGN. We first quantify the Core 1 and 2 O‐glycan structures on the carbohydrate recognition and extracellular domains of the protein using sequential exoglycosidase sequencing. Using ion mobility mass spectrometry, we show how specific O‐glycans, and/or single monosaccharide substitutions, alter both the overall collision cross section and the gas‐phase stability of the DC‐SIGN isoforms. We find that rather than the mass or length of glycoprotein modifications, the stability of DC‐SIGN is better correlated with the number of glycosylation sites.
https://ift.tt/38z6XB8
Journal of the American Chemical SocietyDOI: 10.1021/jacs.0c05644
https://ift.tt/2F7jUqX
I don't want to step on anybody's toes here, but the amount of non-dad jokes here in this subreddit really annoys me. First of all, dad jokes CAN be NSFW, it clearly says so in the sub rules. Secondly, it doesn't automatically make it a dad joke if it's from a conversation between you and your child. Most importantly, the jokes that your CHILDREN tell YOU are not dad jokes. The point of a dad joke is that it's so cheesy only a dad who's trying to be funny would make such a joke. That's it. They are stupid plays on words, lame puns and so on. There has to be a clever pun or wordplay for it to be considered a dad joke.
Again, to all the fellow dads, I apologise if I'm sounding too harsh. But I just needed to get it off my chest.
Do your worst!
I'm surprised it hasn't decade.
For context I'm a Refuse Driver (Garbage man) & today I was on food waste. After I'd tipped I was checking the wagon for any defects when I spotted a lone pea balanced on the lifts.
I said "hey look, an escaPEA"
No one near me but it didn't half make me laugh for a good hour or so!
Edit: I can't believe how much this has blown up. Thank you everyone I've had a blast reading through the replies 😂
It really does, I swear!
Because she wanted to see the task manager.
They’re on standbi
Pilot on me!!
Nothing, he was gladiator.
Dad jokes are supposed to be jokes you can tell a kid and they will understand it and find it funny.
This sub is mostly just NSFW puns now.
If it needs a NSFW tag it's not a dad joke. There should just be a NSFW puns subreddit for that.
Edit* I'm not replying any longer and turning off notifications but to all those that say "no one cares", there sure are a lot of you arguing about it. Maybe I'm wrong but you people don't need to be rude about it. If you really don't care, don't comment.
When I got home, they were still there.
What did 0 say to 8 ?
" Nice Belt "
So What did 3 say to 8 ?
" Hey, you two stop making out "
I won't be doing that today!
[Removed]
Where ever you left it 🤷♀️🤭
This morning, my 4 year old daughter.
Daughter: I'm hungry
Me: nerves building, smile widening
Me: Hi hungry, I'm dad.
She had no idea what was going on but I finally did it.
Thank you all for listening.
You take away their little brooms
There hasn't been a post all year!
It was about a weak back.
SARS‐CoV‐2 attaches to its host receptor, angiotensin‐converting enzyme 2 (ACE2), via the receptor‐binding domain (RBD) of the spike protein. The RBD glycoprotein is a critical target for the development of neutralizing antibodies and vaccines against SARS‐CoV‐2. However, the high heterogeneity of RBD glycoforms may lead to an incomplete neutralization effect and impact the immunogenic integrity of RBD‐based vaccines. Investigating the role of different carbohydrate domains is of paramount importance. Unfortunately, there is no viable method for preparing RBD glycoproteins with structurally defined glycans. Herein we describe a highly efficient and scalable strategy for the preparation of six glycosylated RBDs bearing defined structure glycoforms at T323, N331 and N343. A combination of modern oligosaccharide, peptide synthesis and recombinant protein engineering provides a robust route to deciphering carbohydrate structure−function relationships.
https://ift.tt/30CAAhI
Journal of the American Chemical SocietyDOI: 10.1021/jacs.1c02382
Hongxiang Wu, Yiwei Zhang, Yuanxin Li, Jianchao Xu, Yu Wang, and Xuechen Li
https://ift.tt/3fdtzL7
The first chemical synthesis of homogeneous glycoforms of the SARS-CoV-2 spike receptor-binding domain (RBD) has been accomplished via the combination of protein and carbohydrate chemistry. This strategy provides a versatile synthetic platform for homogeneous glycosylated RBDs of the SARS-CoV-2 S protein and other related virus proteins and a powerful tool for investigating the functions of RBD glycans.
Abstract
SARS-CoV-2 attaches to its host receptor, angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD) of the spike protein. The RBD glycoprotein is a critical target for the development of neutralizing antibodies and vaccines against SARS-CoV-2. However, the high heterogeneity of RBD glycoforms may lead to an incomplete neutralization effect and impact the immunogenic integrity of RBD-based vaccines. Investigating the role of different carbohydrate domains is of paramount importance. Unfortunately, there is no viable method for preparing RBD glycoproteins with structurally defined glycans. Herein we describe a highly efficient and scalable strategy for the preparation of six glycosylated RBDs bearing defined structure glycoforms at T323, N331, and N343. A combination of modern oligosaccharide, peptide synthesis and recombinant protein engineering provides a robust route to decipher carbohydrate structure-function relationships.
https://ift.tt/30CAAhI
